atpαs  (Jena Bioscience)


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  • 92
    Name:
    ATPαS
    Description:

    Catalog Number:
    nu-408l
    Price:
    480.87
    Applications:
    Crystal structure in complex with adenylyl cyclase[1] Activation of beta-cell adenylyl cyclase[2] Potent agonist for P2Y11-receptor[3] Full agonist for rP2Y1-receptor[4]
    Purity:
    ≥ 95 % (HPLC)
    Category:
    Nucleotides Nucleosides
    Buy from Supplier


    Structured Review

    Jena Bioscience atpαs
    Crystal structure of CaAC in complex with <t>ATPαS.</t> a CaAC (E497K/C566D) homodimers form an intertwined helical superstructure within the crystal lattice (blue, red, gray indicate individual superhelices, yellow indicates 8 homodimers within a single asymmetric unit). b Each homodimer consists of two antiparallel arranged monomers and harbors 2 active sites at the dimer interface, occupied by the ATP analog: ATP-Sp-αS. Arrows indicate β4/5 loops, N-termini are labeled, chain A: blue/green, chain B: green/red. c Comparison of the β4/5 loop orientation in CaAC. Overlay of the six monomers of CaAC found in the loop-proximal (green) position close to the catalytic core, or the loop-distal (orange) position. The protein backbone is visualized as a ribbon with selected residues and the base head group shown as sticks. d CaAC active site; the adenine base and phosphate tail of ATP-Sp-αS are anchored by different monomers. Residues of the phosphate binding monomer are marked (*). The previously mutated residues E497K (orange), C566D (red) form hydrogen bonds to the adenine base. The ribose is tilted perpendicular to the adenine plane and points towards β2*, β3*. The conserved arginine, R577 (α4) orients towards Pα. The ion B site is occupied by Ca 2+ , which is octahedrally coordinated among others by two conserved aspartates, D457* and D501*. The phosphate tail of ATP-Sp-αS is anchored to the α1/ β1-loop via polar interactions. mFo-DFc omit map for ATP-Sp-αS contoured at 5σ, contour level is shown as gray mesh. e Magnification of the adenine base binding residues. Neighboring residues of D566, situated on β5 and mutated in RhACs-6 × are colored in red. f Magnification of the residues, involved in nucleotide phosphate binding, coloring as in d . Gray dashed lines indicate hydrogen bonds or metal coordination between 2.3 Å and 3.6 Å in length

    https://www.bioz.com/result/atpαs/product/Jena Bioscience
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    atpαs - by Bioz Stars, 2020-08
    92/100 stars

    Images

    1) Product Images from "Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain"

    Article Title: Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain

    Journal: Nature Communications

    doi: 10.1038/s41467-018-04428-w

    Crystal structure of CaAC in complex with ATPαS. a CaAC (E497K/C566D) homodimers form an intertwined helical superstructure within the crystal lattice (blue, red, gray indicate individual superhelices, yellow indicates 8 homodimers within a single asymmetric unit). b Each homodimer consists of two antiparallel arranged monomers and harbors 2 active sites at the dimer interface, occupied by the ATP analog: ATP-Sp-αS. Arrows indicate β4/5 loops, N-termini are labeled, chain A: blue/green, chain B: green/red. c Comparison of the β4/5 loop orientation in CaAC. Overlay of the six monomers of CaAC found in the loop-proximal (green) position close to the catalytic core, or the loop-distal (orange) position. The protein backbone is visualized as a ribbon with selected residues and the base head group shown as sticks. d CaAC active site; the adenine base and phosphate tail of ATP-Sp-αS are anchored by different monomers. Residues of the phosphate binding monomer are marked (*). The previously mutated residues E497K (orange), C566D (red) form hydrogen bonds to the adenine base. The ribose is tilted perpendicular to the adenine plane and points towards β2*, β3*. The conserved arginine, R577 (α4) orients towards Pα. The ion B site is occupied by Ca 2+ , which is octahedrally coordinated among others by two conserved aspartates, D457* and D501*. The phosphate tail of ATP-Sp-αS is anchored to the α1/ β1-loop via polar interactions. mFo-DFc omit map for ATP-Sp-αS contoured at 5σ, contour level is shown as gray mesh. e Magnification of the adenine base binding residues. Neighboring residues of D566, situated on β5 and mutated in RhACs-6 × are colored in red. f Magnification of the residues, involved in nucleotide phosphate binding, coloring as in d . Gray dashed lines indicate hydrogen bonds or metal coordination between 2.3 Å and 3.6 Å in length
    Figure Legend Snippet: Crystal structure of CaAC in complex with ATPαS. a CaAC (E497K/C566D) homodimers form an intertwined helical superstructure within the crystal lattice (blue, red, gray indicate individual superhelices, yellow indicates 8 homodimers within a single asymmetric unit). b Each homodimer consists of two antiparallel arranged monomers and harbors 2 active sites at the dimer interface, occupied by the ATP analog: ATP-Sp-αS. Arrows indicate β4/5 loops, N-termini are labeled, chain A: blue/green, chain B: green/red. c Comparison of the β4/5 loop orientation in CaAC. Overlay of the six monomers of CaAC found in the loop-proximal (green) position close to the catalytic core, or the loop-distal (orange) position. The protein backbone is visualized as a ribbon with selected residues and the base head group shown as sticks. d CaAC active site; the adenine base and phosphate tail of ATP-Sp-αS are anchored by different monomers. Residues of the phosphate binding monomer are marked (*). The previously mutated residues E497K (orange), C566D (red) form hydrogen bonds to the adenine base. The ribose is tilted perpendicular to the adenine plane and points towards β2*, β3*. The conserved arginine, R577 (α4) orients towards Pα. The ion B site is occupied by Ca 2+ , which is octahedrally coordinated among others by two conserved aspartates, D457* and D501*. The phosphate tail of ATP-Sp-αS is anchored to the α1/ β1-loop via polar interactions. mFo-DFc omit map for ATP-Sp-αS contoured at 5σ, contour level is shown as gray mesh. e Magnification of the adenine base binding residues. Neighboring residues of D566, situated on β5 and mutated in RhACs-6 × are colored in red. f Magnification of the residues, involved in nucleotide phosphate binding, coloring as in d . Gray dashed lines indicate hydrogen bonds or metal coordination between 2.3 Å and 3.6 Å in length

    Techniques Used: Labeling, Binding Assay

    2) Product Images from "Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain"

    Article Title: Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain

    Journal: Nature Communications

    doi: 10.1038/s41467-018-04428-w

    Crystal structure of CaAC in complex with ATPαS. a CaAC (E497K/C566D) homodimers form an intertwined helical superstructure within the crystal lattice (blue, red, gray indicate individual superhelices, yellow indicates 8 homodimers within a single asymmetric unit). b Each homodimer consists of two antiparallel arranged monomers and harbors 2 active sites at the dimer interface, occupied by the ATP analog: ATP-Sp-αS. Arrows indicate β4/5 loops, N-termini are labeled, chain A: blue/green, chain B: green/red. c Comparison of the β4/5 loop orientation in CaAC. Overlay of the six monomers of CaAC found in the loop-proximal (green) position close to the catalytic core, or the loop-distal (orange) position. The protein backbone is visualized as a ribbon with selected residues and the base head group shown as sticks. d CaAC active site; the adenine base and phosphate tail of ATP-Sp-αS are anchored by different monomers. Residues of the phosphate binding monomer are marked (*). The previously mutated residues E497K (orange), C566D (red) form hydrogen bonds to the adenine base. The ribose is tilted perpendicular to the adenine plane and points towards β2*, β3*. The conserved arginine, R577 (α4) orients towards Pα. The ion B site is occupied by Ca 2+ , which is octahedrally coordinated among others by two conserved aspartates, D457* and D501*. The phosphate tail of ATP-Sp-αS is anchored to the α1/ β1-loop via polar interactions. mFo-DFc omit map for ATP-Sp-αS contoured at 5σ, contour level is shown as gray mesh. e Magnification of the adenine base binding residues. Neighboring residues of D566, situated on β5 and mutated in RhACs-6 × are colored in red. f Magnification of the residues, involved in nucleotide phosphate binding, coloring as in d . Gray dashed lines indicate hydrogen bonds or metal coordination between 2.3 Å and 3.6 Å in length
    Figure Legend Snippet: Crystal structure of CaAC in complex with ATPαS. a CaAC (E497K/C566D) homodimers form an intertwined helical superstructure within the crystal lattice (blue, red, gray indicate individual superhelices, yellow indicates 8 homodimers within a single asymmetric unit). b Each homodimer consists of two antiparallel arranged monomers and harbors 2 active sites at the dimer interface, occupied by the ATP analog: ATP-Sp-αS. Arrows indicate β4/5 loops, N-termini are labeled, chain A: blue/green, chain B: green/red. c Comparison of the β4/5 loop orientation in CaAC. Overlay of the six monomers of CaAC found in the loop-proximal (green) position close to the catalytic core, or the loop-distal (orange) position. The protein backbone is visualized as a ribbon with selected residues and the base head group shown as sticks. d CaAC active site; the adenine base and phosphate tail of ATP-Sp-αS are anchored by different monomers. Residues of the phosphate binding monomer are marked (*). The previously mutated residues E497K (orange), C566D (red) form hydrogen bonds to the adenine base. The ribose is tilted perpendicular to the adenine plane and points towards β2*, β3*. The conserved arginine, R577 (α4) orients towards Pα. The ion B site is occupied by Ca 2+ , which is octahedrally coordinated among others by two conserved aspartates, D457* and D501*. The phosphate tail of ATP-Sp-αS is anchored to the α1/ β1-loop via polar interactions. mFo-DFc omit map for ATP-Sp-αS contoured at 5σ, contour level is shown as gray mesh. e Magnification of the adenine base binding residues. Neighboring residues of D566, situated on β5 and mutated in RhACs-6 × are colored in red. f Magnification of the residues, involved in nucleotide phosphate binding, coloring as in d . Gray dashed lines indicate hydrogen bonds or metal coordination between 2.3 Å and 3.6 Å in length

    Techniques Used: Labeling, Binding Assay

    Related Articles

    Crystallization Assay:

    Article Title: Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain
    Article Snippet: .. Crystallization and structure solution of cyclases The cyclase domain CaAC (E497K/C566D) was co-crystalized with ATPαS (Jena Bioscience) at 20 °C. ..

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  • 92
    Jena Bioscience atpαs
    Crystal structure of CaAC in complex with <t>ATPαS.</t> a CaAC (E497K/C566D) homodimers form an intertwined helical superstructure within the crystal lattice (blue, red, gray indicate individual superhelices, yellow indicates 8 homodimers within a single asymmetric unit). b Each homodimer consists of two antiparallel arranged monomers and harbors 2 active sites at the dimer interface, occupied by the ATP analog: ATP-Sp-αS. Arrows indicate β4/5 loops, N-termini are labeled, chain A: blue/green, chain B: green/red. c Comparison of the β4/5 loop orientation in CaAC. Overlay of the six monomers of CaAC found in the loop-proximal (green) position close to the catalytic core, or the loop-distal (orange) position. The protein backbone is visualized as a ribbon with selected residues and the base head group shown as sticks. d CaAC active site; the adenine base and phosphate tail of ATP-Sp-αS are anchored by different monomers. Residues of the phosphate binding monomer are marked (*). The previously mutated residues E497K (orange), C566D (red) form hydrogen bonds to the adenine base. The ribose is tilted perpendicular to the adenine plane and points towards β2*, β3*. The conserved arginine, R577 (α4) orients towards Pα. The ion B site is occupied by Ca 2+ , which is octahedrally coordinated among others by two conserved aspartates, D457* and D501*. The phosphate tail of ATP-Sp-αS is anchored to the α1/ β1-loop via polar interactions. mFo-DFc omit map for ATP-Sp-αS contoured at 5σ, contour level is shown as gray mesh. e Magnification of the adenine base binding residues. Neighboring residues of D566, situated on β5 and mutated in RhACs-6 × are colored in red. f Magnification of the residues, involved in nucleotide phosphate binding, coloring as in d . Gray dashed lines indicate hydrogen bonds or metal coordination between 2.3 Å and 3.6 Å in length
    Atpαs, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/atpαs/product/Jena Bioscience
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    atpαs - by Bioz Stars, 2020-08
    92/100 stars
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    Crystal structure of CaAC in complex with ATPαS. a CaAC (E497K/C566D) homodimers form an intertwined helical superstructure within the crystal lattice (blue, red, gray indicate individual superhelices, yellow indicates 8 homodimers within a single asymmetric unit). b Each homodimer consists of two antiparallel arranged monomers and harbors 2 active sites at the dimer interface, occupied by the ATP analog: ATP-Sp-αS. Arrows indicate β4/5 loops, N-termini are labeled, chain A: blue/green, chain B: green/red. c Comparison of the β4/5 loop orientation in CaAC. Overlay of the six monomers of CaAC found in the loop-proximal (green) position close to the catalytic core, or the loop-distal (orange) position. The protein backbone is visualized as a ribbon with selected residues and the base head group shown as sticks. d CaAC active site; the adenine base and phosphate tail of ATP-Sp-αS are anchored by different monomers. Residues of the phosphate binding monomer are marked (*). The previously mutated residues E497K (orange), C566D (red) form hydrogen bonds to the adenine base. The ribose is tilted perpendicular to the adenine plane and points towards β2*, β3*. The conserved arginine, R577 (α4) orients towards Pα. The ion B site is occupied by Ca 2+ , which is octahedrally coordinated among others by two conserved aspartates, D457* and D501*. The phosphate tail of ATP-Sp-αS is anchored to the α1/ β1-loop via polar interactions. mFo-DFc omit map for ATP-Sp-αS contoured at 5σ, contour level is shown as gray mesh. e Magnification of the adenine base binding residues. Neighboring residues of D566, situated on β5 and mutated in RhACs-6 × are colored in red. f Magnification of the residues, involved in nucleotide phosphate binding, coloring as in d . Gray dashed lines indicate hydrogen bonds or metal coordination between 2.3 Å and 3.6 Å in length

    Journal: Nature Communications

    Article Title: Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain

    doi: 10.1038/s41467-018-04428-w

    Figure Lengend Snippet: Crystal structure of CaAC in complex with ATPαS. a CaAC (E497K/C566D) homodimers form an intertwined helical superstructure within the crystal lattice (blue, red, gray indicate individual superhelices, yellow indicates 8 homodimers within a single asymmetric unit). b Each homodimer consists of two antiparallel arranged monomers and harbors 2 active sites at the dimer interface, occupied by the ATP analog: ATP-Sp-αS. Arrows indicate β4/5 loops, N-termini are labeled, chain A: blue/green, chain B: green/red. c Comparison of the β4/5 loop orientation in CaAC. Overlay of the six monomers of CaAC found in the loop-proximal (green) position close to the catalytic core, or the loop-distal (orange) position. The protein backbone is visualized as a ribbon with selected residues and the base head group shown as sticks. d CaAC active site; the adenine base and phosphate tail of ATP-Sp-αS are anchored by different monomers. Residues of the phosphate binding monomer are marked (*). The previously mutated residues E497K (orange), C566D (red) form hydrogen bonds to the adenine base. The ribose is tilted perpendicular to the adenine plane and points towards β2*, β3*. The conserved arginine, R577 (α4) orients towards Pα. The ion B site is occupied by Ca 2+ , which is octahedrally coordinated among others by two conserved aspartates, D457* and D501*. The phosphate tail of ATP-Sp-αS is anchored to the α1/ β1-loop via polar interactions. mFo-DFc omit map for ATP-Sp-αS contoured at 5σ, contour level is shown as gray mesh. e Magnification of the adenine base binding residues. Neighboring residues of D566, situated on β5 and mutated in RhACs-6 × are colored in red. f Magnification of the residues, involved in nucleotide phosphate binding, coloring as in d . Gray dashed lines indicate hydrogen bonds or metal coordination between 2.3 Å and 3.6 Å in length

    Article Snippet: Crystallization and structure solution of cyclases The cyclase domain CaAC (E497K/C566D) was co-crystalized with ATPαS (Jena Bioscience) at 20 °C.

    Techniques: Labeling, Binding Assay

    Crystal structure of CaAC in complex with ATPαS. a CaAC (E497K/C566D) homodimers form an intertwined helical superstructure within the crystal lattice (blue, red, gray indicate individual superhelices, yellow indicates 8 homodimers within a single asymmetric unit). b Each homodimer consists of two antiparallel arranged monomers and harbors 2 active sites at the dimer interface, occupied by the ATP analog: ATP-Sp-αS. Arrows indicate β4/5 loops, N-termini are labeled, chain A: blue/green, chain B: green/red. c Comparison of the β4/5 loop orientation in CaAC. Overlay of the six monomers of CaAC found in the loop-proximal (green) position close to the catalytic core, or the loop-distal (orange) position. The protein backbone is visualized as a ribbon with selected residues and the base head group shown as sticks. d CaAC active site; the adenine base and phosphate tail of ATP-Sp-αS are anchored by different monomers. Residues of the phosphate binding monomer are marked (*). The previously mutated residues E497K (orange), C566D (red) form hydrogen bonds to the adenine base. The ribose is tilted perpendicular to the adenine plane and points towards β2*, β3*. The conserved arginine, R577 (α4) orients towards Pα. The ion B site is occupied by Ca 2+ , which is octahedrally coordinated among others by two conserved aspartates, D457* and D501*. The phosphate tail of ATP-Sp-αS is anchored to the α1/ β1-loop via polar interactions. mFo-DFc omit map for ATP-Sp-αS contoured at 5σ, contour level is shown as gray mesh. e Magnification of the adenine base binding residues. Neighboring residues of D566, situated on β5 and mutated in RhACs-6 × are colored in red. f Magnification of the residues, involved in nucleotide phosphate binding, coloring as in d . Gray dashed lines indicate hydrogen bonds or metal coordination between 2.3 Å and 3.6 Å in length

    Journal: Nature Communications

    Article Title: Rhodopsin-cyclases for photocontrol of cGMP/cAMP and 2.3 Å structure of the adenylyl cyclase domain

    doi: 10.1038/s41467-018-04428-w

    Figure Lengend Snippet: Crystal structure of CaAC in complex with ATPαS. a CaAC (E497K/C566D) homodimers form an intertwined helical superstructure within the crystal lattice (blue, red, gray indicate individual superhelices, yellow indicates 8 homodimers within a single asymmetric unit). b Each homodimer consists of two antiparallel arranged monomers and harbors 2 active sites at the dimer interface, occupied by the ATP analog: ATP-Sp-αS. Arrows indicate β4/5 loops, N-termini are labeled, chain A: blue/green, chain B: green/red. c Comparison of the β4/5 loop orientation in CaAC. Overlay of the six monomers of CaAC found in the loop-proximal (green) position close to the catalytic core, or the loop-distal (orange) position. The protein backbone is visualized as a ribbon with selected residues and the base head group shown as sticks. d CaAC active site; the adenine base and phosphate tail of ATP-Sp-αS are anchored by different monomers. Residues of the phosphate binding monomer are marked (*). The previously mutated residues E497K (orange), C566D (red) form hydrogen bonds to the adenine base. The ribose is tilted perpendicular to the adenine plane and points towards β2*, β3*. The conserved arginine, R577 (α4) orients towards Pα. The ion B site is occupied by Ca 2+ , which is octahedrally coordinated among others by two conserved aspartates, D457* and D501*. The phosphate tail of ATP-Sp-αS is anchored to the α1/ β1-loop via polar interactions. mFo-DFc omit map for ATP-Sp-αS contoured at 5σ, contour level is shown as gray mesh. e Magnification of the adenine base binding residues. Neighboring residues of D566, situated on β5 and mutated in RhACs-6 × are colored in red. f Magnification of the residues, involved in nucleotide phosphate binding, coloring as in d . Gray dashed lines indicate hydrogen bonds or metal coordination between 2.3 Å and 3.6 Å in length

    Article Snippet: The cyclase domain CaAC (E497K/C566D) was co-crystalized with ATPαS (Jena Bioscience) at 20 °C.

    Techniques: Labeling, Binding Assay