3 d 2 mant gtp  (Jena Bioscience)


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    Name:
    Mant GTP
    Description:

    Catalog Number:
    nu-206l
    Price:
    343.57
    Applications:
    Inhibition of AC-isoform[1] and GTPs[2] Activity measurement: GC[3] Specifity measurements with isoforms of ACs[4] FRET: AC[5], edema factor[6] Inhibition of edema factor (anthrax)[6]
    Purity:
    ≥ 95 % (HPLC)
    Category:
    Nucleotides Nucleosides
    Buy from Supplier


    Structured Review

    Jena Bioscience 3 d 2 mant gtp
    Fluorescence emission spectra of <t>2’-MANT-</t> and 3’-MANT-nucleotides bound to VC1:VC1 homodimer: Comparison with <t>MANT-GTP</t> and MANT-ATP

    https://www.bioz.com/result/3 d 2 mant gtp/product/Jena Bioscience
    Average 93 stars, based on 61 article reviews
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    3 d 2 mant gtp - by Bioz Stars, 2020-08
    93/100 stars

    Images

    1) Product Images from "Structure-Activity Relationships for the Interactions of 2'- and 3'-(O)-(N-Methyl)anthraniloyl-Substituted Purine and Pyrimidine Nucleotides with Mammalian Adenylyl Cyclases"

    Article Title: Structure-Activity Relationships for the Interactions of 2'- and 3'-(O)-(N-Methyl)anthraniloyl-Substituted Purine and Pyrimidine Nucleotides with Mammalian Adenylyl Cyclases

    Journal: Biochemical pharmacology

    doi: 10.1016/j.bcp.2011.05.010

    Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:VC1 homodimer: Comparison with MANT-GTP and MANT-ATP
    Figure Legend Snippet: Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:VC1 homodimer: Comparison with MANT-GTP and MANT-ATP

    Techniques Used: Fluorescence

    Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:IIC2 heterodimer: Comparison with MANT-GTP and MANT-ATP
    Figure Legend Snippet: Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:IIC2 heterodimer: Comparison with MANT-GTP and MANT-ATP

    Techniques Used: Fluorescence

    2) Product Images from "A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNACys"

    Article Title: A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNACys

    Journal: Journal of Structural and Functional Genomics

    doi: 10.1007/s10969-015-9193-6

    Close-up stereo views of the switch I and II regions in EF-Tu ( a ) and MM1309 ( b ). The bound GMPPNP molecule and the Mg 2+ ion, and the EF-Tu and MM1309 residues in the switch I and II regions, which are involved in the GMPPNP interactions, are shown as stick models. The EF-Tu and MM1309 residues that are involved in the domain–domain interactions are also shown as stick models. The switch I and II regions of MM1309 are involved in domain–domain interactions, rather than GTP/GDP interactions. The switch I and II regions are colored pink and green , respectively. Transparent ribbon models of EF-Tu ( blue ) and MM1309 ( white ) are visible in the background
    Figure Legend Snippet: Close-up stereo views of the switch I and II regions in EF-Tu ( a ) and MM1309 ( b ). The bound GMPPNP molecule and the Mg 2+ ion, and the EF-Tu and MM1309 residues in the switch I and II regions, which are involved in the GMPPNP interactions, are shown as stick models. The EF-Tu and MM1309 residues that are involved in the domain–domain interactions are also shown as stick models. The switch I and II regions of MM1309 are involved in domain–domain interactions, rather than GTP/GDP interactions. The switch I and II regions are colored pink and green , respectively. Transparent ribbon models of EF-Tu ( blue ) and MM1309 ( white ) are visible in the background

    Techniques Used:

    ITC analysis. The upper and lower panels display the ITC titration curves and the binding isotherms, respectively, for MM1309 with GTP·Mg 2+ ( a ), GTP without Mg 2+ ( b ), GDP·Mg 2+ ( c ), and GMPPNP·Mg 2+ ( d ). N , the binding stoichiometry; K b , the observed binding constant; K d ( K d = 1/ K b ), the dissociation constant; ∆ H , the binding enthalpy; ∆ S , the binding entropy
    Figure Legend Snippet: ITC analysis. The upper and lower panels display the ITC titration curves and the binding isotherms, respectively, for MM1309 with GTP·Mg 2+ ( a ), GTP without Mg 2+ ( b ), GDP·Mg 2+ ( c ), and GMPPNP·Mg 2+ ( d ). N , the binding stoichiometry; K b , the observed binding constant; K d ( K d = 1/ K b ), the dissociation constant; ∆ H , the binding enthalpy; ∆ S , the binding entropy

    Techniques Used: Titration, Binding Assay

    Stereo views of the GTP binding sites. a The bound GMPPNP molecule in the T. aquaticus EF-Tu·GMPPNP·Mg 2+ structure. b The bound GMPPNP molecule in the MM1309·GMPPNP·Mg 2+ structure. The F o – F c omit map (contoured at 3.3 σ) of the bound GMPPNP·Mg 2+ in the MM1309 active site. c , d Close-up stereo views around the γ-phosphate group of the bound GMPPNP in T. aquaticus EF-Tu·GMPPNP·Mg 2+ ( c ) and MM1309·GMPPNP·Mg 2+ ( d ). The amino acid residues surrounding the phosphate groups and the magnesium ions of the bound GMPPNP·Mg 2+ are depicted by stick models. e The bound GDP molecule in the MM1309·GDP structure. The F o – F c omit map (contoured at 4.0 σ) of the bound GDP·Mg 2+ in the MM1309 active site. f The GTP binding site in the MM1309 apo form. The MM1309 residues that are located close to the bound guanine nucleotide are represented as stick models. The P-loop motifs (Gly17–Thr25 in EF-Tu and Gly7–Thr15 in MM1309) are shown in sky blue . The switch I regions are colored pink . Transparent ribbon models of EF-Tu ( blue ) and MM1309 ( white ) are visible in the background
    Figure Legend Snippet: Stereo views of the GTP binding sites. a The bound GMPPNP molecule in the T. aquaticus EF-Tu·GMPPNP·Mg 2+ structure. b The bound GMPPNP molecule in the MM1309·GMPPNP·Mg 2+ structure. The F o – F c omit map (contoured at 3.3 σ) of the bound GMPPNP·Mg 2+ in the MM1309 active site. c , d Close-up stereo views around the γ-phosphate group of the bound GMPPNP in T. aquaticus EF-Tu·GMPPNP·Mg 2+ ( c ) and MM1309·GMPPNP·Mg 2+ ( d ). The amino acid residues surrounding the phosphate groups and the magnesium ions of the bound GMPPNP·Mg 2+ are depicted by stick models. e The bound GDP molecule in the MM1309·GDP structure. The F o – F c omit map (contoured at 4.0 σ) of the bound GDP·Mg 2+ in the MM1309 active site. f The GTP binding site in the MM1309 apo form. The MM1309 residues that are located close to the bound guanine nucleotide are represented as stick models. The P-loop motifs (Gly17–Thr25 in EF-Tu and Gly7–Thr15 in MM1309) are shown in sky blue . The switch I regions are colored pink . Transparent ribbon models of EF-Tu ( blue ) and MM1309 ( white ) are visible in the background

    Techniques Used: Binding Assay

    Superposition of MM1309 with EF-Tu, aSelB, and aIF2γ, represented by ribbon models. a Superposition of the MM1309 structures in the GMPPNP-bound, GDP-bound, and apo forms. b Superposition of MM1309 with T. aquaticus EF-Tu in the GTP-bound form (PDB code: 1TTT). c Superposition of MM1309 with T. aquaticus EF-Tu in the GDP-bound form (PDB code: 1TUI). d Superposition of MM1309 with M. maripaludis aSelB (PDB code: 4ACA) and with P. abyssi aIF2γ (PDB code: 1KK0)
    Figure Legend Snippet: Superposition of MM1309 with EF-Tu, aSelB, and aIF2γ, represented by ribbon models. a Superposition of the MM1309 structures in the GMPPNP-bound, GDP-bound, and apo forms. b Superposition of MM1309 with T. aquaticus EF-Tu in the GTP-bound form (PDB code: 1TTT). c Superposition of MM1309 with T. aquaticus EF-Tu in the GDP-bound form (PDB code: 1TUI). d Superposition of MM1309 with M. maripaludis aSelB (PDB code: 4ACA) and with P. abyssi aIF2γ (PDB code: 1KK0)

    Techniques Used:

    3) Product Images from "The activation mechanism of Irga6, an interferon-inducible GTPase contributing to mouse resistance against Toxoplasma gondii"

    Article Title: The activation mechanism of Irga6, an interferon-inducible GTPase contributing to mouse resistance against Toxoplasma gondii

    Journal: BMC Biology

    doi: 10.1186/1741-7007-9-7

    The Glu106 is essential for the activation of GTP hydrolysis . (a and b) View of the nucleotide-binding region. (a) The Irga6 dimer model (Figure 4) is shown (cyan and magenta). The cis interaction between the Glu106 and the γ-phosphate, and the putative trans interactions between the 3'OH and Glu106, as well as between the 3'OH and the γ-phosphate are represented by dotted lines. (b) Two molecules (cyan and magenta) of Irga6 bound to GDP (PDB 1TPZ/A ) [ 14 ] were adjusted to the Irga6 dimer model, to give the best overlay for the G1, G3, G4 and G5-motifs. The resulting theoretical model of the
    Figure Legend Snippet: The Glu106 is essential for the activation of GTP hydrolysis . (a and b) View of the nucleotide-binding region. (a) The Irga6 dimer model (Figure 4) is shown (cyan and magenta). The cis interaction between the Glu106 and the γ-phosphate, and the putative trans interactions between the 3'OH and Glu106, as well as between the 3'OH and the γ-phosphate are represented by dotted lines. (b) Two molecules (cyan and magenta) of Irga6 bound to GDP (PDB 1TPZ/A ) [ 14 ] were adjusted to the Irga6 dimer model, to give the best overlay for the G1, G3, G4 and G5-motifs. The resulting theoretical model of the "Irga6 dimer in the GDP state" is shown. (c) Oligomerisation of 80 μM WT or mutant Irga6 proteins was monitored by light scattering in the presence of 10 mM GTP at 37°C. (d) Hydrolysis of 10 mM GTP (with traces α 32 P-GTP) was measured in the presence of 80 μM WT or mutant Irga6 proteins at 37°C. Samples were assayed by TLC and autoradiography.

    Techniques Used: Activation Assay, Binding Assay, Mutagenesis, Thin Layer Chromatography, Autoradiography

    The nucleotide base is part of the catalytic interface . (a and b) View of the nucleotide-binding region. The Irga6 dimer model (Figure 4) is shown. Glu77, Ser132 (magenta), Asp186 (cyan), of WT Irga6, with two GppNHp nucleotides (a) and modeled Asn186 (cyan), of Irga6-D186N, with two XTP nucleotides (b) are shown. The interactions of Asp186 with GppNHp and of Asn186 with XTP are represented by dotted lines. (c) Oligomerisation of 80 μM Irga6-D186N protein was monitored by light scattering in the presence of 10 mM GTP at 37°C. The experiment was performed with and without the addition of 1 mM XTP. (d) Hydrolysis of 10 mM GTP (with traces α 32 P-GTP) was measured in the presence of 80 μM Irga6-D186N protein at 37°C. The experiment was performed with and without the addition of 1 mM XTP. Samples were assayed by TLC and autoradiography.
    Figure Legend Snippet: The nucleotide base is part of the catalytic interface . (a and b) View of the nucleotide-binding region. The Irga6 dimer model (Figure 4) is shown. Glu77, Ser132 (magenta), Asp186 (cyan), of WT Irga6, with two GppNHp nucleotides (a) and modeled Asn186 (cyan), of Irga6-D186N, with two XTP nucleotides (b) are shown. The interactions of Asp186 with GppNHp and of Asn186 with XTP are represented by dotted lines. (c) Oligomerisation of 80 μM Irga6-D186N protein was monitored by light scattering in the presence of 10 mM GTP at 37°C. The experiment was performed with and without the addition of 1 mM XTP. (d) Hydrolysis of 10 mM GTP (with traces α 32 P-GTP) was measured in the presence of 80 μM Irga6-D186N protein at 37°C. The experiment was performed with and without the addition of 1 mM XTP. Samples were assayed by TLC and autoradiography.

    Techniques Used: Binding Assay, Thin Layer Chromatography, Autoradiography

    4) Product Images from "Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation †"

    Article Title: Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation †

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkq1250

    UMPKmt activity versus Mg-ATP concentration. Enzyme activity was determined at a fixed concentration of UMP (2 mM), and, in the absence (filled square) or in the presence of effectors (0.5 mM GTP: filled circle and 0.1 mM UTP: diamond-shaped). The curves correspond to the fit of the experimental data to the Hill equation and the calculated parameters are displayed in Table 2 .
    Figure Legend Snippet: UMPKmt activity versus Mg-ATP concentration. Enzyme activity was determined at a fixed concentration of UMP (2 mM), and, in the absence (filled square) or in the presence of effectors (0.5 mM GTP: filled circle and 0.1 mM UTP: diamond-shaped). The curves correspond to the fit of the experimental data to the Hill equation and the calculated parameters are displayed in Table 2 .

    Techniques Used: Activity Assay, Concentration Assay

    F81W and F81W S96A variant activity versus Mg-ATP concentration. The concentrations of effectors were 0.5 mM GTP (dark blue), 1 mM GTP (light blue), no effector (red), 0.2 mM UTP (dark green) and 1 mM UTP (light green). Same conditions as Figure 1 .
    Figure Legend Snippet: F81W and F81W S96A variant activity versus Mg-ATP concentration. The concentrations of effectors were 0.5 mM GTP (dark blue), 1 mM GTP (light blue), no effector (red), 0.2 mM UTP (dark green) and 1 mM UTP (light green). Same conditions as Figure 1 .

    Techniques Used: Variant Assay, Activity Assay, Concentration Assay

    Effect of the effectors on UMPKmt activity. ( A ). Enzyme activity was determined at fixed concentrations of substrates (5 mM Mg-ATP and 2 mM UMP) in the absence (filled circle) or in the presence (filled square) of 0.5 mM UTP. Each data point represents a single determination. ( B ). Same as (A) but with GTP as the effector.
    Figure Legend Snippet: Effect of the effectors on UMPKmt activity. ( A ). Enzyme activity was determined at fixed concentrations of substrates (5 mM Mg-ATP and 2 mM UMP) in the absence (filled circle) or in the presence (filled square) of 0.5 mM UTP. Each data point represents a single determination. ( B ). Same as (A) but with GTP as the effector.

    Techniques Used: Activity Assay

    P139W, P139H and P139A variant activity versus Mg-ATP concentration. The concentrations of effectors were 2 mM GTP (light blue), 0.5 mM GTP (dark blue), no effector (red), 0.5 mM UTP (dark green), 1 mM UTP (light green) and 2 mM UTP (gold green). Same conditions as Figure 1 .
    Figure Legend Snippet: P139W, P139H and P139A variant activity versus Mg-ATP concentration. The concentrations of effectors were 2 mM GTP (light blue), 0.5 mM GTP (dark blue), no effector (red), 0.5 mM UTP (dark green), 1 mM UTP (light green) and 2 mM UTP (gold green). Same conditions as Figure 1 .

    Techniques Used: Variant Assay, Activity Assay, Concentration Assay

    5) Product Images from "Structure-Activity Relationships for the Interactions of 2'- and 3'-(O)-(N-Methyl)anthraniloyl-Substituted Purine and Pyrimidine Nucleotides with Mammalian Adenylyl Cyclases"

    Article Title: Structure-Activity Relationships for the Interactions of 2'- and 3'-(O)-(N-Methyl)anthraniloyl-Substituted Purine and Pyrimidine Nucleotides with Mammalian Adenylyl Cyclases

    Journal: Biochemical pharmacology

    doi: 10.1016/j.bcp.2011.05.010

    Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:VC1 homodimer: Comparison with MANT-GTP and MANT-ATP
    Figure Legend Snippet: Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:VC1 homodimer: Comparison with MANT-GTP and MANT-ATP

    Techniques Used: Fluorescence

    Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:IIC2 heterodimer: Comparison with MANT-GTP and MANT-ATP
    Figure Legend Snippet: Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:IIC2 heterodimer: Comparison with MANT-GTP and MANT-ATP

    Techniques Used: Fluorescence

    6) Product Images from "Structural Basis for the High-Affinity Inhibition of Mammalian Membranous Adenylyl Cyclase by 2?,3?-O-(N-Methylanthraniloyl)-Inosine 5?-Triphosphate S⃞"

    Article Title: Structural Basis for the High-Affinity Inhibition of Mammalian Membranous Adenylyl Cyclase by 2?,3?-O-(N-Methylanthraniloyl)-Inosine 5?-Triphosphate S⃞

    Journal: Molecular Pharmacology

    doi: 10.1124/mol.111.071894

    Comparison of the binding of MANT-ITP and MANT-GTP by molecular dynamics simulations. Overlaid graphical representations of the terminal ( t = 9.6 ns) time steps for the MANT-GTP (CPK-colored sticks with green carbons and orange phosphorus atoms) and MANT-ITP (CPK-colored sticks with cyan carbons and tan phosphorus atoms) interacting with the VC1:IIC2 receptor (pale green ribbons) and its cofactor Mn 2+ ions (magenta spheres for MANT-GTP simulation and purple for MANT-ITP). Additional details on differences in the interactions of MANT-GTP and MANT-ITP with VC1:IIC2 are provided in Supplemental Fig. 1 and Supplemental Tables 1 to 3.
    Figure Legend Snippet: Comparison of the binding of MANT-ITP and MANT-GTP by molecular dynamics simulations. Overlaid graphical representations of the terminal ( t = 9.6 ns) time steps for the MANT-GTP (CPK-colored sticks with green carbons and orange phosphorus atoms) and MANT-ITP (CPK-colored sticks with cyan carbons and tan phosphorus atoms) interacting with the VC1:IIC2 receptor (pale green ribbons) and its cofactor Mn 2+ ions (magenta spheres for MANT-GTP simulation and purple for MANT-ITP). Additional details on differences in the interactions of MANT-GTP and MANT-ITP with VC1:IIC2 are provided in Supplemental Fig. 1 and Supplemental Tables 1 to 3.

    Techniques Used: Binding Assay

    Structure of MANT nucleoside 5′-triphosphates (NTPs). Represented are MANT-ITP, MANT-GTP, and MANT-XTP, the MANT nucleotides used for enzymatic studies, fluorescence spectroscopy, crystallography, and structure activity evaluation. The MANT group isomerizes between the 2′ and 3′- O -ribosyl function. Note the different substitution of the C2 carbon atom of the purine ring in the various nucleotides.
    Figure Legend Snippet: Structure of MANT nucleoside 5′-triphosphates (NTPs). Represented are MANT-ITP, MANT-GTP, and MANT-XTP, the MANT nucleotides used for enzymatic studies, fluorescence spectroscopy, crystallography, and structure activity evaluation. The MANT group isomerizes between the 2′ and 3′- O -ribosyl function. Note the different substitution of the C2 carbon atom of the purine ring in the various nucleotides.

    Techniques Used: Fluorescence, Spectroscopy, Activity Assay

    Binding mode of MANT-ITP and two Mn 2+ ions in the catalytic site. MANT-ITP and two metal ions are bound in the cleft between the soluble C1a and C2a domains. VC1 and IIC2 are colored wheat and light pink, respectively. MANT-ITP is shown as stick model, carbon atoms are cyan, nitrogen atoms are dark blue, oxygen atoms are red, and phosphorus atoms are green. The two Mn 2+ ions are shown as orange spheres. A, difference electron density for 3′- O -MANT-ITP and Mn 2+ . The lime green wire represents the |F o |-|F c | electron density for MANT-ITP contoured at 2.5 σ. The blue wire corresponds to the |F o |-|F c | electron density for the two Mn 2+ ). B, detailed view of substrate binding site of VC1:IIC2 with MANT-ITP:Mn 2+ . The catalytic site of VC1:IIC2 shows MANT-ITP, A- and B- site of two Mn 2+ ions and the protein residues that are responsible for ligand interaction. The interaction among protein residues and MANT-ITP, Mn 2+ are shown as dashed gray lines. C, superimposed crystal structures of 3′- O ). The protein residues are in almost identical conformation, and the inhibitors are situated in the substrate binding pocket in a similar fashion. D, superimposed purine binding site of 3′- O -MANT-ITP and 3′-O-MANT-GTP. The interaction of the hypoxanthine ring and guanine ring of MANT-ITP and MANT-GTP are shown as dashed black and olive green lines, respectively. The distances of hydrogen bond between the hypoxanthine ring and surrounding protein residues of MANT-ITP are indicated in Ångstroms. The hydrogen bond between Ile1019 and the amino group of MANT-GTP is missing in the MANT-ITP structure. Lys938 and the oxygen of the hypoxanthine ring are further apart. The hypoxanthine ring has less binding constraint in the purine binding pocket in comparison to the guanine ring of MANT-GTP.
    Figure Legend Snippet: Binding mode of MANT-ITP and two Mn 2+ ions in the catalytic site. MANT-ITP and two metal ions are bound in the cleft between the soluble C1a and C2a domains. VC1 and IIC2 are colored wheat and light pink, respectively. MANT-ITP is shown as stick model, carbon atoms are cyan, nitrogen atoms are dark blue, oxygen atoms are red, and phosphorus atoms are green. The two Mn 2+ ions are shown as orange spheres. A, difference electron density for 3′- O -MANT-ITP and Mn 2+ . The lime green wire represents the |F o |-|F c | electron density for MANT-ITP contoured at 2.5 σ. The blue wire corresponds to the |F o |-|F c | electron density for the two Mn 2+ ). B, detailed view of substrate binding site of VC1:IIC2 with MANT-ITP:Mn 2+ . The catalytic site of VC1:IIC2 shows MANT-ITP, A- and B- site of two Mn 2+ ions and the protein residues that are responsible for ligand interaction. The interaction among protein residues and MANT-ITP, Mn 2+ are shown as dashed gray lines. C, superimposed crystal structures of 3′- O ). The protein residues are in almost identical conformation, and the inhibitors are situated in the substrate binding pocket in a similar fashion. D, superimposed purine binding site of 3′- O -MANT-ITP and 3′-O-MANT-GTP. The interaction of the hypoxanthine ring and guanine ring of MANT-ITP and MANT-GTP are shown as dashed black and olive green lines, respectively. The distances of hydrogen bond between the hypoxanthine ring and surrounding protein residues of MANT-ITP are indicated in Ångstroms. The hydrogen bond between Ile1019 and the amino group of MANT-GTP is missing in the MANT-ITP structure. Lys938 and the oxygen of the hypoxanthine ring are further apart. The hypoxanthine ring has less binding constraint in the purine binding pocket in comparison to the guanine ring of MANT-GTP.

    Techniques Used: Binding Assay

    MANT-binding site. A detailed view of the MANT-binding site is depicted. MANT-ITP is shown as a stick model; carbon atoms are cyan, nitrogen atoms are dark blue, oxygen atoms are red and one phosphorus atom is displayed in green. VC1 and IIC2 are colored wheat and light pink, respectively. MANT-GTP is shown as a transparent yellow stick model. The carbonyl group of MANT-ITP is in closer contact to Asn1025 but does not interact with the side chain of Asn1025 in this orientation. Apart from this, no conformational differences between MANT-ITP and MANT-GTP are detected. However, MANT-ITP might exert stronger hydrophobic interactions due to changes of the relative positions of Trp1020 and the MANT group.
    Figure Legend Snippet: MANT-binding site. A detailed view of the MANT-binding site is depicted. MANT-ITP is shown as a stick model; carbon atoms are cyan, nitrogen atoms are dark blue, oxygen atoms are red and one phosphorus atom is displayed in green. VC1 and IIC2 are colored wheat and light pink, respectively. MANT-GTP is shown as a transparent yellow stick model. The carbonyl group of MANT-ITP is in closer contact to Asn1025 but does not interact with the side chain of Asn1025 in this orientation. Apart from this, no conformational differences between MANT-ITP and MANT-GTP are detected. However, MANT-ITP might exert stronger hydrophobic interactions due to changes of the relative positions of Trp1020 and the MANT group.

    Techniques Used: Binding Assay

    7) Product Images from "Structure-Activity Relationships for the Interactions of 2'- and 3'-(O)-(N-Methyl)anthraniloyl-Substituted Purine and Pyrimidine Nucleotides with Mammalian Adenylyl Cyclases"

    Article Title: Structure-Activity Relationships for the Interactions of 2'- and 3'-(O)-(N-Methyl)anthraniloyl-Substituted Purine and Pyrimidine Nucleotides with Mammalian Adenylyl Cyclases

    Journal: Biochemical pharmacology

    doi: 10.1016/j.bcp.2011.05.010

    Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:VC1 homodimer: Comparison with MANT-GTP and MANT-ATP
    Figure Legend Snippet: Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:VC1 homodimer: Comparison with MANT-GTP and MANT-ATP

    Techniques Used: Fluorescence

    Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:IIC2 heterodimer: Comparison with MANT-GTP and MANT-ATP
    Figure Legend Snippet: Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:IIC2 heterodimer: Comparison with MANT-GTP and MANT-ATP

    Techniques Used: Fluorescence

    8) Product Images from "Differential Interactions of the Catalytic Subunits of Adenylyl Cyclase with Forskolin Analogs"

    Article Title: Differential Interactions of the Catalytic Subunits of Adenylyl Cyclase with Forskolin Analogs

    Journal: Biochemical pharmacology

    doi: 10.1016/j.bcp.2009.03.023

    Cumulative concentration/response curves for the effects of FS on FRET and direct MANT-GTP fluorescence in C1/C2
    Figure Legend Snippet: Cumulative concentration/response curves for the effects of FS on FRET and direct MANT-GTP fluorescence in C1/C2

    Techniques Used: Concentration Assay, Fluorescence

    Effects of FS and FS analogs on FRET and direct MANT-GTP fluorescence in C1/C2
    Figure Legend Snippet: Effects of FS and FS analogs on FRET and direct MANT-GTP fluorescence in C1/C2

    Techniques Used: Fluorescence

    Efficacies of FS and FS analogs at stimulating direct MANT-GTP fluorescence and at inducing FRET in C1/C2
    Figure Legend Snippet: Efficacies of FS and FS analogs at stimulating direct MANT-GTP fluorescence and at inducing FRET in C1/C2

    Techniques Used: Fluorescence

    9) Product Images from "Biophysical basis of cellular multi-specificity encoded in a model molecular switch"

    Article Title: Biophysical basis of cellular multi-specificity encoded in a model molecular switch

    Journal: bioRxiv

    doi: 10.1101/2020.01.04.893909

    Gsp1 interface mutations act allosterically to modulate the rate of GTP hydrolysis. a , Annotated 1D 31 P NMR spectrum of wild-type Gsp1 loaded with GTP. Peak areas are computed over intervals shown and normalized to the GTPβ bound (GTPβbound) peak. The peaks from left to right correspond to: free phosphate (Pi), β phosphate of GDP bound to Gsp1 (GDPβbound), β phosphate of free (unbound) GDP (GDPβfree), γ phosphate of GTP bound to Gsp1 in conformation 1 (γ1), γ phosphate of GTP bound to Gsp1 in conformation 2 (γ2), α phosphate of bound or unbound GDP or GTP, β phosphate of GTP bound to Gsp1 (GTPβbound), β phosphate of free (unbound) GTP (GTPβfree). b , Rate of intrinsic GTP hydrolysis of wild-type Gsp1 and mutants. Dotted line indicates wild-type value. Error bars represent the standard deviations from n 3 replicates (except for A180T which has two replicates). c , Percent population in γ2 state plotted against the relative rate of intrinsic GTP hydrolysis represented as a natural logarithm of the ratio of the rate for the mutant over the rate of the wild type. The pink line is a linear fit. Error bars represent the standard deviation from n 3 replicates of intrinsic GTP hydrolysis measurements (except for A180T which has two replicates). d , Structures of HRas (in cartoon representation, blue) bound to allosteric inhibitors shown in stick representation: BI 2852 (PDB ID: 6gj8, light violet), vinylsulfonamide (PDB ID: 4m1w, dark violet), and AMG 510 (PDB ID: 6oim, deepsalmon). Switch I and switch II regions of HRas are in green and yellow, respectively. Human HRas residues corresponding to Gsp1 allosteric sites (identified from the sequence alignment between Gsp1 and human HRas) are represented as pink spheres. The corresponding Gsp1 residues are in parentheses.
    Figure Legend Snippet: Gsp1 interface mutations act allosterically to modulate the rate of GTP hydrolysis. a , Annotated 1D 31 P NMR spectrum of wild-type Gsp1 loaded with GTP. Peak areas are computed over intervals shown and normalized to the GTPβ bound (GTPβbound) peak. The peaks from left to right correspond to: free phosphate (Pi), β phosphate of GDP bound to Gsp1 (GDPβbound), β phosphate of free (unbound) GDP (GDPβfree), γ phosphate of GTP bound to Gsp1 in conformation 1 (γ1), γ phosphate of GTP bound to Gsp1 in conformation 2 (γ2), α phosphate of bound or unbound GDP or GTP, β phosphate of GTP bound to Gsp1 (GTPβbound), β phosphate of free (unbound) GTP (GTPβfree). b , Rate of intrinsic GTP hydrolysis of wild-type Gsp1 and mutants. Dotted line indicates wild-type value. Error bars represent the standard deviations from n 3 replicates (except for A180T which has two replicates). c , Percent population in γ2 state plotted against the relative rate of intrinsic GTP hydrolysis represented as a natural logarithm of the ratio of the rate for the mutant over the rate of the wild type. The pink line is a linear fit. Error bars represent the standard deviation from n 3 replicates of intrinsic GTP hydrolysis measurements (except for A180T which has two replicates). d , Structures of HRas (in cartoon representation, blue) bound to allosteric inhibitors shown in stick representation: BI 2852 (PDB ID: 6gj8, light violet), vinylsulfonamide (PDB ID: 4m1w, dark violet), and AMG 510 (PDB ID: 6oim, deepsalmon). Switch I and switch II regions of HRas are in green and yellow, respectively. Human HRas residues corresponding to Gsp1 allosteric sites (identified from the sequence alignment between Gsp1 and human HRas) are represented as pink spheres. The corresponding Gsp1 residues are in parentheses.

    Techniques Used: Nuclear Magnetic Resonance, Relative Rate, Mutagenesis, Standard Deviation, Sequencing

    Genetic interaction (GI) profiles of Gsp1 interface point mutants cluster by biological processes but not by targeted interfaces. a , Schematic summary of approach combining systems-level and biophysical measurements to characterize functional multi-specificity of a biological switch motif. b , Interface point mutations enable probing of the biological functions of the multi-specific GTPase switch Gsp1. c , Structures of Ran/Gsp1 in the GTP-bound (marine, PDB ID: 1ibr) and GDP-bound (gray, PDB ID: 3gj0) states. Mutated Gsp1 residues are shown as spheres. Switch loops I and II are shown in green and yellow, respectively. d , GI profiles of 23 Gsp1 mutants with nine or more significant GIs. Negative S-score (blue) represents synthetic sick/lethal GIs, positive S-score (yellow) represents suppressive/epistatic GIs. Mutants and genes are hierarchically clustered by Pearson correlation. e , Locations of mutated residues in structurally characterized interfaces. ΔrASA is the difference in accessible surface area of a residue upon binding, relative to an empirical maximum for the solvent accessible surface area of each amino acid residue type computed as in ( 5 ). f , Distributions of significant (see Methods) GIs of Gsp1 point mutants compared to GIs of mutant alleles of essential and non-essential genes. Red bars indicate the mean. g , Distributions of Pearson correlations between the GI profiles of Gsp1 interaction partners and Gsp1 mutants if mutation is (right, black) or is not (left, gray) in the interface with that partner. Point size indicates the false discovery rate adjusted one-sided (positive) p-value of the Pearson correlation. Red dots and bars indicate the mean and the upper and lower quartile, respectively.
    Figure Legend Snippet: Genetic interaction (GI) profiles of Gsp1 interface point mutants cluster by biological processes but not by targeted interfaces. a , Schematic summary of approach combining systems-level and biophysical measurements to characterize functional multi-specificity of a biological switch motif. b , Interface point mutations enable probing of the biological functions of the multi-specific GTPase switch Gsp1. c , Structures of Ran/Gsp1 in the GTP-bound (marine, PDB ID: 1ibr) and GDP-bound (gray, PDB ID: 3gj0) states. Mutated Gsp1 residues are shown as spheres. Switch loops I and II are shown in green and yellow, respectively. d , GI profiles of 23 Gsp1 mutants with nine or more significant GIs. Negative S-score (blue) represents synthetic sick/lethal GIs, positive S-score (yellow) represents suppressive/epistatic GIs. Mutants and genes are hierarchically clustered by Pearson correlation. e , Locations of mutated residues in structurally characterized interfaces. ΔrASA is the difference in accessible surface area of a residue upon binding, relative to an empirical maximum for the solvent accessible surface area of each amino acid residue type computed as in ( 5 ). f , Distributions of significant (see Methods) GIs of Gsp1 point mutants compared to GIs of mutant alleles of essential and non-essential genes. Red bars indicate the mean. g , Distributions of Pearson correlations between the GI profiles of Gsp1 interaction partners and Gsp1 mutants if mutation is (right, black) or is not (left, gray) in the interface with that partner. Point size indicates the false discovery rate adjusted one-sided (positive) p-value of the Pearson correlation. Red dots and bars indicate the mean and the upper and lower quartile, respectively.

    Techniques Used: Functional Assay, Binding Assay, Mutagenesis

    Related Articles

    other:

    Article Title: A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNACys
    Article Snippet: [2′-/3′-O -(N -methylanthraniloyl)guanosine-5′-O -triphosphate] (Mant-GTP) and [2′-/3′-O -(N -methylanthraniloyl)guanosine-5′-O -diphosphate] (Mant-GDP) were purchased from Jena Bioscience (Germany).

    Article Title: The activation mechanism of Irga6, an interferon-inducible GTPase contributing to mouse resistance against Toxoplasma gondii
    Article Snippet: Nucleotides GTP (Carl Roth, Karlsruhe, Germany and Sigma-Aldrich, St.Louis, MO, USA); GDP (Sigma-Aldrich, St.Louis, MO, USA); GTPγS, XTP, 2'deoxy-GTP, mant-GTP, mant-GDP, mant-GTPγS, 2'mant-3'deoxy-GTP, 2'deoxy-3'mant-GTP, mant-XTP and mant-XDP (Jena Bioscience, Jena, Germany); 3'deoxy-GTP (Jena Bioscience, Jena, Germany and Trilink Biotechnologies, San Diego, CA, USA); 2'3'dideoxy-GTP (GE Healthcare, Munich, Germany); α32 P-GTP (GE Healthcare, Munich, Germany, Hartmann Analytic, Braunschweig, Germany and Perkin Elmer, Waltham, MA, USA); γ32 P-3'dGTP (Hartmann Analytic, Braunschweig, Germany)

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    Jena Bioscience 3 d 2 mant gtp
    Fluorescence emission spectra of <t>2’-MANT-</t> and 3’-MANT-nucleotides bound to VC1:VC1 homodimer: Comparison with <t>MANT-GTP</t> and MANT-ATP
    3 D 2 Mant Gtp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 93/100, based on 38 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:VC1 homodimer: Comparison with MANT-GTP and MANT-ATP

    Journal: Biochemical pharmacology

    Article Title: Structure-Activity Relationships for the Interactions of 2'- and 3'-(O)-(N-Methyl)anthraniloyl-Substituted Purine and Pyrimidine Nucleotides with Mammalian Adenylyl Cyclases

    doi: 10.1016/j.bcp.2011.05.010

    Figure Lengend Snippet: Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:VC1 homodimer: Comparison with MANT-GTP and MANT-ATP

    Article Snippet: MANT-GTP ( 1 ), 2’-d-3’-MANT-GTP ( 2 ), 3’-d-2’-MANT-GTP ( 3 ), MANT-GTPγS ( 4 ), MANT-ATP ( 5 ), 2’-d-3’-MANT-ATP ( 6 ), 3’-d-2’-MANT-ATP ( 7 ), MANT-ITPγS ( 9 ), MANT-XTP ( 10 ), ANT-GTP ( 14 ) and MANT-ADP ( 16 ) were obtained from Jena Bioscience (Jena, Germany).

    Techniques: Fluorescence

    Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:IIC2 heterodimer: Comparison with MANT-GTP and MANT-ATP

    Journal: Biochemical pharmacology

    Article Title: Structure-Activity Relationships for the Interactions of 2'- and 3'-(O)-(N-Methyl)anthraniloyl-Substituted Purine and Pyrimidine Nucleotides with Mammalian Adenylyl Cyclases

    doi: 10.1016/j.bcp.2011.05.010

    Figure Lengend Snippet: Fluorescence emission spectra of 2’-MANT- and 3’-MANT-nucleotides bound to VC1:IIC2 heterodimer: Comparison with MANT-GTP and MANT-ATP

    Article Snippet: MANT-GTP ( 1 ), 2’-d-3’-MANT-GTP ( 2 ), 3’-d-2’-MANT-GTP ( 3 ), MANT-GTPγS ( 4 ), MANT-ATP ( 5 ), 2’-d-3’-MANT-ATP ( 6 ), 3’-d-2’-MANT-ATP ( 7 ), MANT-ITPγS ( 9 ), MANT-XTP ( 10 ), ANT-GTP ( 14 ) and MANT-ADP ( 16 ) were obtained from Jena Bioscience (Jena, Germany).

    Techniques: Fluorescence

    Close-up stereo views of the switch I and II regions in EF-Tu ( a ) and MM1309 ( b ). The bound GMPPNP molecule and the Mg 2+ ion, and the EF-Tu and MM1309 residues in the switch I and II regions, which are involved in the GMPPNP interactions, are shown as stick models. The EF-Tu and MM1309 residues that are involved in the domain–domain interactions are also shown as stick models. The switch I and II regions of MM1309 are involved in domain–domain interactions, rather than GTP/GDP interactions. The switch I and II regions are colored pink and green , respectively. Transparent ribbon models of EF-Tu ( blue ) and MM1309 ( white ) are visible in the background

    Journal: Journal of Structural and Functional Genomics

    Article Title: A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNACys

    doi: 10.1007/s10969-015-9193-6

    Figure Lengend Snippet: Close-up stereo views of the switch I and II regions in EF-Tu ( a ) and MM1309 ( b ). The bound GMPPNP molecule and the Mg 2+ ion, and the EF-Tu and MM1309 residues in the switch I and II regions, which are involved in the GMPPNP interactions, are shown as stick models. The EF-Tu and MM1309 residues that are involved in the domain–domain interactions are also shown as stick models. The switch I and II regions of MM1309 are involved in domain–domain interactions, rather than GTP/GDP interactions. The switch I and II regions are colored pink and green , respectively. Transparent ribbon models of EF-Tu ( blue ) and MM1309 ( white ) are visible in the background

    Article Snippet: [2′-/3′-O -(N -methylanthraniloyl)guanosine-5′-O -triphosphate] (Mant-GTP) and [2′-/3′-O -(N -methylanthraniloyl)guanosine-5′-O -diphosphate] (Mant-GDP) were purchased from Jena Bioscience (Germany).

    Techniques:

    ITC analysis. The upper and lower panels display the ITC titration curves and the binding isotherms, respectively, for MM1309 with GTP·Mg 2+ ( a ), GTP without Mg 2+ ( b ), GDP·Mg 2+ ( c ), and GMPPNP·Mg 2+ ( d ). N , the binding stoichiometry; K b , the observed binding constant; K d ( K d = 1/ K b ), the dissociation constant; ∆ H , the binding enthalpy; ∆ S , the binding entropy

    Journal: Journal of Structural and Functional Genomics

    Article Title: A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNACys

    doi: 10.1007/s10969-015-9193-6

    Figure Lengend Snippet: ITC analysis. The upper and lower panels display the ITC titration curves and the binding isotherms, respectively, for MM1309 with GTP·Mg 2+ ( a ), GTP without Mg 2+ ( b ), GDP·Mg 2+ ( c ), and GMPPNP·Mg 2+ ( d ). N , the binding stoichiometry; K b , the observed binding constant; K d ( K d = 1/ K b ), the dissociation constant; ∆ H , the binding enthalpy; ∆ S , the binding entropy

    Article Snippet: [2′-/3′-O -(N -methylanthraniloyl)guanosine-5′-O -triphosphate] (Mant-GTP) and [2′-/3′-O -(N -methylanthraniloyl)guanosine-5′-O -diphosphate] (Mant-GDP) were purchased from Jena Bioscience (Germany).

    Techniques: Titration, Binding Assay

    Stereo views of the GTP binding sites. a The bound GMPPNP molecule in the T. aquaticus EF-Tu·GMPPNP·Mg 2+ structure. b The bound GMPPNP molecule in the MM1309·GMPPNP·Mg 2+ structure. The F o – F c omit map (contoured at 3.3 σ) of the bound GMPPNP·Mg 2+ in the MM1309 active site. c , d Close-up stereo views around the γ-phosphate group of the bound GMPPNP in T. aquaticus EF-Tu·GMPPNP·Mg 2+ ( c ) and MM1309·GMPPNP·Mg 2+ ( d ). The amino acid residues surrounding the phosphate groups and the magnesium ions of the bound GMPPNP·Mg 2+ are depicted by stick models. e The bound GDP molecule in the MM1309·GDP structure. The F o – F c omit map (contoured at 4.0 σ) of the bound GDP·Mg 2+ in the MM1309 active site. f The GTP binding site in the MM1309 apo form. The MM1309 residues that are located close to the bound guanine nucleotide are represented as stick models. The P-loop motifs (Gly17–Thr25 in EF-Tu and Gly7–Thr15 in MM1309) are shown in sky blue . The switch I regions are colored pink . Transparent ribbon models of EF-Tu ( blue ) and MM1309 ( white ) are visible in the background

    Journal: Journal of Structural and Functional Genomics

    Article Title: A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNACys

    doi: 10.1007/s10969-015-9193-6

    Figure Lengend Snippet: Stereo views of the GTP binding sites. a The bound GMPPNP molecule in the T. aquaticus EF-Tu·GMPPNP·Mg 2+ structure. b The bound GMPPNP molecule in the MM1309·GMPPNP·Mg 2+ structure. The F o – F c omit map (contoured at 3.3 σ) of the bound GMPPNP·Mg 2+ in the MM1309 active site. c , d Close-up stereo views around the γ-phosphate group of the bound GMPPNP in T. aquaticus EF-Tu·GMPPNP·Mg 2+ ( c ) and MM1309·GMPPNP·Mg 2+ ( d ). The amino acid residues surrounding the phosphate groups and the magnesium ions of the bound GMPPNP·Mg 2+ are depicted by stick models. e The bound GDP molecule in the MM1309·GDP structure. The F o – F c omit map (contoured at 4.0 σ) of the bound GDP·Mg 2+ in the MM1309 active site. f The GTP binding site in the MM1309 apo form. The MM1309 residues that are located close to the bound guanine nucleotide are represented as stick models. The P-loop motifs (Gly17–Thr25 in EF-Tu and Gly7–Thr15 in MM1309) are shown in sky blue . The switch I regions are colored pink . Transparent ribbon models of EF-Tu ( blue ) and MM1309 ( white ) are visible in the background

    Article Snippet: [2′-/3′-O -(N -methylanthraniloyl)guanosine-5′-O -triphosphate] (Mant-GTP) and [2′-/3′-O -(N -methylanthraniloyl)guanosine-5′-O -diphosphate] (Mant-GDP) were purchased from Jena Bioscience (Germany).

    Techniques: Binding Assay

    Superposition of MM1309 with EF-Tu, aSelB, and aIF2γ, represented by ribbon models. a Superposition of the MM1309 structures in the GMPPNP-bound, GDP-bound, and apo forms. b Superposition of MM1309 with T. aquaticus EF-Tu in the GTP-bound form (PDB code: 1TTT). c Superposition of MM1309 with T. aquaticus EF-Tu in the GDP-bound form (PDB code: 1TUI). d Superposition of MM1309 with M. maripaludis aSelB (PDB code: 4ACA) and with P. abyssi aIF2γ (PDB code: 1KK0)

    Journal: Journal of Structural and Functional Genomics

    Article Title: A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNACys

    doi: 10.1007/s10969-015-9193-6

    Figure Lengend Snippet: Superposition of MM1309 with EF-Tu, aSelB, and aIF2γ, represented by ribbon models. a Superposition of the MM1309 structures in the GMPPNP-bound, GDP-bound, and apo forms. b Superposition of MM1309 with T. aquaticus EF-Tu in the GTP-bound form (PDB code: 1TTT). c Superposition of MM1309 with T. aquaticus EF-Tu in the GDP-bound form (PDB code: 1TUI). d Superposition of MM1309 with M. maripaludis aSelB (PDB code: 4ACA) and with P. abyssi aIF2γ (PDB code: 1KK0)

    Article Snippet: [2′-/3′-O -(N -methylanthraniloyl)guanosine-5′-O -triphosphate] (Mant-GTP) and [2′-/3′-O -(N -methylanthraniloyl)guanosine-5′-O -diphosphate] (Mant-GDP) were purchased from Jena Bioscience (Germany).

    Techniques:

    The Glu106 is essential for the activation of GTP hydrolysis . (a and b) View of the nucleotide-binding region. (a) The Irga6 dimer model (Figure 4) is shown (cyan and magenta). The cis interaction between the Glu106 and the γ-phosphate, and the putative trans interactions between the 3'OH and Glu106, as well as between the 3'OH and the γ-phosphate are represented by dotted lines. (b) Two molecules (cyan and magenta) of Irga6 bound to GDP (PDB 1TPZ/A ) [ 14 ] were adjusted to the Irga6 dimer model, to give the best overlay for the G1, G3, G4 and G5-motifs. The resulting theoretical model of the

    Journal: BMC Biology

    Article Title: The activation mechanism of Irga6, an interferon-inducible GTPase contributing to mouse resistance against Toxoplasma gondii

    doi: 10.1186/1741-7007-9-7

    Figure Lengend Snippet: The Glu106 is essential for the activation of GTP hydrolysis . (a and b) View of the nucleotide-binding region. (a) The Irga6 dimer model (Figure 4) is shown (cyan and magenta). The cis interaction between the Glu106 and the γ-phosphate, and the putative trans interactions between the 3'OH and Glu106, as well as between the 3'OH and the γ-phosphate are represented by dotted lines. (b) Two molecules (cyan and magenta) of Irga6 bound to GDP (PDB 1TPZ/A ) [ 14 ] were adjusted to the Irga6 dimer model, to give the best overlay for the G1, G3, G4 and G5-motifs. The resulting theoretical model of the "Irga6 dimer in the GDP state" is shown. (c) Oligomerisation of 80 μM WT or mutant Irga6 proteins was monitored by light scattering in the presence of 10 mM GTP at 37°C. (d) Hydrolysis of 10 mM GTP (with traces α 32 P-GTP) was measured in the presence of 80 μM WT or mutant Irga6 proteins at 37°C. Samples were assayed by TLC and autoradiography.

    Article Snippet: Nucleotides GTP (Carl Roth, Karlsruhe, Germany and Sigma-Aldrich, St.Louis, MO, USA); GDP (Sigma-Aldrich, St.Louis, MO, USA); GTPγS, XTP, 2'deoxy-GTP, mant-GTP, mant-GDP, mant-GTPγS, 2'mant-3'deoxy-GTP, 2'deoxy-3'mant-GTP, mant-XTP and mant-XDP (Jena Bioscience, Jena, Germany); 3'deoxy-GTP (Jena Bioscience, Jena, Germany and Trilink Biotechnologies, San Diego, CA, USA); 2'3'dideoxy-GTP (GE Healthcare, Munich, Germany); α32 P-GTP (GE Healthcare, Munich, Germany, Hartmann Analytic, Braunschweig, Germany and Perkin Elmer, Waltham, MA, USA); γ32 P-3'dGTP (Hartmann Analytic, Braunschweig, Germany)

    Techniques: Activation Assay, Binding Assay, Mutagenesis, Thin Layer Chromatography, Autoradiography

    The nucleotide base is part of the catalytic interface . (a and b) View of the nucleotide-binding region. The Irga6 dimer model (Figure 4) is shown. Glu77, Ser132 (magenta), Asp186 (cyan), of WT Irga6, with two GppNHp nucleotides (a) and modeled Asn186 (cyan), of Irga6-D186N, with two XTP nucleotides (b) are shown. The interactions of Asp186 with GppNHp and of Asn186 with XTP are represented by dotted lines. (c) Oligomerisation of 80 μM Irga6-D186N protein was monitored by light scattering in the presence of 10 mM GTP at 37°C. The experiment was performed with and without the addition of 1 mM XTP. (d) Hydrolysis of 10 mM GTP (with traces α 32 P-GTP) was measured in the presence of 80 μM Irga6-D186N protein at 37°C. The experiment was performed with and without the addition of 1 mM XTP. Samples were assayed by TLC and autoradiography.

    Journal: BMC Biology

    Article Title: The activation mechanism of Irga6, an interferon-inducible GTPase contributing to mouse resistance against Toxoplasma gondii

    doi: 10.1186/1741-7007-9-7

    Figure Lengend Snippet: The nucleotide base is part of the catalytic interface . (a and b) View of the nucleotide-binding region. The Irga6 dimer model (Figure 4) is shown. Glu77, Ser132 (magenta), Asp186 (cyan), of WT Irga6, with two GppNHp nucleotides (a) and modeled Asn186 (cyan), of Irga6-D186N, with two XTP nucleotides (b) are shown. The interactions of Asp186 with GppNHp and of Asn186 with XTP are represented by dotted lines. (c) Oligomerisation of 80 μM Irga6-D186N protein was monitored by light scattering in the presence of 10 mM GTP at 37°C. The experiment was performed with and without the addition of 1 mM XTP. (d) Hydrolysis of 10 mM GTP (with traces α 32 P-GTP) was measured in the presence of 80 μM Irga6-D186N protein at 37°C. The experiment was performed with and without the addition of 1 mM XTP. Samples were assayed by TLC and autoradiography.

    Article Snippet: Nucleotides GTP (Carl Roth, Karlsruhe, Germany and Sigma-Aldrich, St.Louis, MO, USA); GDP (Sigma-Aldrich, St.Louis, MO, USA); GTPγS, XTP, 2'deoxy-GTP, mant-GTP, mant-GDP, mant-GTPγS, 2'mant-3'deoxy-GTP, 2'deoxy-3'mant-GTP, mant-XTP and mant-XDP (Jena Bioscience, Jena, Germany); 3'deoxy-GTP (Jena Bioscience, Jena, Germany and Trilink Biotechnologies, San Diego, CA, USA); 2'3'dideoxy-GTP (GE Healthcare, Munich, Germany); α32 P-GTP (GE Healthcare, Munich, Germany, Hartmann Analytic, Braunschweig, Germany and Perkin Elmer, Waltham, MA, USA); γ32 P-3'dGTP (Hartmann Analytic, Braunschweig, Germany)

    Techniques: Binding Assay, Thin Layer Chromatography, Autoradiography

    UMPKmt activity versus Mg-ATP concentration. Enzyme activity was determined at a fixed concentration of UMP (2 mM), and, in the absence (filled square) or in the presence of effectors (0.5 mM GTP: filled circle and 0.1 mM UTP: diamond-shaped). The curves correspond to the fit of the experimental data to the Hill equation and the calculated parameters are displayed in Table 2 .

    Journal: Nucleic Acids Research

    Article Title: Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation †

    doi: 10.1093/nar/gkq1250

    Figure Lengend Snippet: UMPKmt activity versus Mg-ATP concentration. Enzyme activity was determined at a fixed concentration of UMP (2 mM), and, in the absence (filled square) or in the presence of effectors (0.5 mM GTP: filled circle and 0.1 mM UTP: diamond-shaped). The curves correspond to the fit of the experimental data to the Hill equation and the calculated parameters are displayed in Table 2 .

    Article Snippet: 5F-UMP, 5Br-UMP, 5F-UTP, 5I-UTP, aminoallyl UTP, 8Br-GTP, Mant-GTP, 6-methylthio GTP, GMPPCP and GMPPNP were purchased from Jena Bioscience.

    Techniques: Activity Assay, Concentration Assay

    F81W and F81W S96A variant activity versus Mg-ATP concentration. The concentrations of effectors were 0.5 mM GTP (dark blue), 1 mM GTP (light blue), no effector (red), 0.2 mM UTP (dark green) and 1 mM UTP (light green). Same conditions as Figure 1 .

    Journal: Nucleic Acids Research

    Article Title: Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation †

    doi: 10.1093/nar/gkq1250

    Figure Lengend Snippet: F81W and F81W S96A variant activity versus Mg-ATP concentration. The concentrations of effectors were 0.5 mM GTP (dark blue), 1 mM GTP (light blue), no effector (red), 0.2 mM UTP (dark green) and 1 mM UTP (light green). Same conditions as Figure 1 .

    Article Snippet: 5F-UMP, 5Br-UMP, 5F-UTP, 5I-UTP, aminoallyl UTP, 8Br-GTP, Mant-GTP, 6-methylthio GTP, GMPPCP and GMPPNP were purchased from Jena Bioscience.

    Techniques: Variant Assay, Activity Assay, Concentration Assay

    Effect of the effectors on UMPKmt activity. ( A ). Enzyme activity was determined at fixed concentrations of substrates (5 mM Mg-ATP and 2 mM UMP) in the absence (filled circle) or in the presence (filled square) of 0.5 mM UTP. Each data point represents a single determination. ( B ). Same as (A) but with GTP as the effector.

    Journal: Nucleic Acids Research

    Article Title: Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation †

    doi: 10.1093/nar/gkq1250

    Figure Lengend Snippet: Effect of the effectors on UMPKmt activity. ( A ). Enzyme activity was determined at fixed concentrations of substrates (5 mM Mg-ATP and 2 mM UMP) in the absence (filled circle) or in the presence (filled square) of 0.5 mM UTP. Each data point represents a single determination. ( B ). Same as (A) but with GTP as the effector.

    Article Snippet: 5F-UMP, 5Br-UMP, 5F-UTP, 5I-UTP, aminoallyl UTP, 8Br-GTP, Mant-GTP, 6-methylthio GTP, GMPPCP and GMPPNP were purchased from Jena Bioscience.

    Techniques: Activity Assay

    P139W, P139H and P139A variant activity versus Mg-ATP concentration. The concentrations of effectors were 2 mM GTP (light blue), 0.5 mM GTP (dark blue), no effector (red), 0.5 mM UTP (dark green), 1 mM UTP (light green) and 2 mM UTP (gold green). Same conditions as Figure 1 .

    Journal: Nucleic Acids Research

    Article Title: Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation †

    doi: 10.1093/nar/gkq1250

    Figure Lengend Snippet: P139W, P139H and P139A variant activity versus Mg-ATP concentration. The concentrations of effectors were 2 mM GTP (light blue), 0.5 mM GTP (dark blue), no effector (red), 0.5 mM UTP (dark green), 1 mM UTP (light green) and 2 mM UTP (gold green). Same conditions as Figure 1 .

    Article Snippet: 5F-UMP, 5Br-UMP, 5F-UTP, 5I-UTP, aminoallyl UTP, 8Br-GTP, Mant-GTP, 6-methylthio GTP, GMPPCP and GMPPNP were purchased from Jena Bioscience.

    Techniques: Variant Assay, Activity Assay, Concentration Assay