adpβs  (Jena Bioscience)


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  • 92
    Name:
    ADPβS
    Description:

    Catalog Number:
    NU-433-25
    Price:
    369.6
    Category:
    Nucleotides Nucleosides
    Size:
    25 mg
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    Structured Review

    Jena Bioscience adpβs
    Structural comparison between MacB vs. Sav1866 and PglK. Ribbon representation of (left) ADP-bound, outward-open conformation of Sav1866 (blue, PDB accession code: 2HYD) 9 , (middle) ADP bound, outward-occluded conformation of PglK (orange, PDB accession code:5C73) 25 and (right) <t>ADPβS-bound</t> MacB (green), viewed from membrane plane (top) and cytoplasm (bottom). Dotted lines depict the approximate membrane boundaries. Alfa phosphate atoms of the two bound nucleotides are connected by a magenta line showing the interface in each NBD dimer. For ADP-bound PglK, the coordinates of ADP were not deposited in the Protein Data Bank 25 . Outward-facing, V-shaped cavities in the TMDs are depicted as dotted triangles. Elbow helix and connecting TM1, which contribute to the extent of the external opening in each transporter, are coloured in red

    https://www.bioz.com/result/adpβs/product/Jena Bioscience
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    adpβs - by Bioz Stars, 2021-06
    92/100 stars

    Images

    1) Product Images from "Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii"

    Article Title: Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii

    Journal: Nature Communications

    doi: 10.1038/s41467-017-01399-2

    Structural comparison between MacB vs. Sav1866 and PglK. Ribbon representation of (left) ADP-bound, outward-open conformation of Sav1866 (blue, PDB accession code: 2HYD) 9 , (middle) ADP bound, outward-occluded conformation of PglK (orange, PDB accession code:5C73) 25 and (right) ADPβS-bound MacB (green), viewed from membrane plane (top) and cytoplasm (bottom). Dotted lines depict the approximate membrane boundaries. Alfa phosphate atoms of the two bound nucleotides are connected by a magenta line showing the interface in each NBD dimer. For ADP-bound PglK, the coordinates of ADP were not deposited in the Protein Data Bank 25 . Outward-facing, V-shaped cavities in the TMDs are depicted as dotted triangles. Elbow helix and connecting TM1, which contribute to the extent of the external opening in each transporter, are coloured in red
    Figure Legend Snippet: Structural comparison between MacB vs. Sav1866 and PglK. Ribbon representation of (left) ADP-bound, outward-open conformation of Sav1866 (blue, PDB accession code: 2HYD) 9 , (middle) ADP bound, outward-occluded conformation of PglK (orange, PDB accession code:5C73) 25 and (right) ADPβS-bound MacB (green), viewed from membrane plane (top) and cytoplasm (bottom). Dotted lines depict the approximate membrane boundaries. Alfa phosphate atoms of the two bound nucleotides are connected by a magenta line showing the interface in each NBD dimer. For ADP-bound PglK, the coordinates of ADP were not deposited in the Protein Data Bank 25 . Outward-facing, V-shaped cavities in the TMDs are depicted as dotted triangles. Elbow helix and connecting TM1, which contribute to the extent of the external opening in each transporter, are coloured in red

    Techniques Used:

    Nucleotide-binding sites in MacB dimer. a NBD dimer and b close-up view of an ATP-binding site interacting with ADPβS. Each monomer in dimeric MacB is coloured in green and red, respectively. Walker A motif in cyan, and carboxy-terminal coupling helix (CH2) in yellow, LSGGQ motif in ABC signature in orange. The difference Fourier map F o– F c (without ADPβS) contoured at 2 σ ( σ is the root mean square electron density of the map) (shown in blue cage) and the anomalous difference Fourier map contoured at 4 σ (shown in red cage) for phosphor and sulphur atoms of bound ADPβS. Bound ADPβS is shown in stick representation in a and b with the positions of the C, N, O, P and S atoms indicated by yellow, blue, red, orange and gold, respectively. The positions of key residues of nucleotide-binding site in b are also shown in stick representation with the position of the C atoms indicated in green. c Structural comparison of NBDs in different nucleotide-bound states. Side view (top row) and top–down view on NBDs (bottom row). Superimposition of the right half of NBD dimers of MacB (green) vs. AMP-PNP-bound Sav1866 from S. aureus (PDB accession code: 2ONJ in blue) 60 , AMP-PNP-bound MsbA from Salmonella typhimurium (PDB accession code: 3B60 in magenta) 10 , ADP-bound PglK from C. jejuni (PDB accession code: 5C73 in red) 25 , closed apo-form MsbA from V. cholera (PDB accession code: 3B5X in magenta) 10 or open apo-form MsbA from E. coli (PDB accession code: 3B5W in magenta) 10 (Supplementary Table 1 ). Attempts to superimpose the Mac-NBD on the NBDs of other ABC transporters, such as ABC importers and heterodimeric ABC exporters, were less successful due to differences in the number of helices and the distinct configurations of the NBDs
    Figure Legend Snippet: Nucleotide-binding sites in MacB dimer. a NBD dimer and b close-up view of an ATP-binding site interacting with ADPβS. Each monomer in dimeric MacB is coloured in green and red, respectively. Walker A motif in cyan, and carboxy-terminal coupling helix (CH2) in yellow, LSGGQ motif in ABC signature in orange. The difference Fourier map F o– F c (without ADPβS) contoured at 2 σ ( σ is the root mean square electron density of the map) (shown in blue cage) and the anomalous difference Fourier map contoured at 4 σ (shown in red cage) for phosphor and sulphur atoms of bound ADPβS. Bound ADPβS is shown in stick representation in a and b with the positions of the C, N, O, P and S atoms indicated by yellow, blue, red, orange and gold, respectively. The positions of key residues of nucleotide-binding site in b are also shown in stick representation with the position of the C atoms indicated in green. c Structural comparison of NBDs in different nucleotide-bound states. Side view (top row) and top–down view on NBDs (bottom row). Superimposition of the right half of NBD dimers of MacB (green) vs. AMP-PNP-bound Sav1866 from S. aureus (PDB accession code: 2ONJ in blue) 60 , AMP-PNP-bound MsbA from Salmonella typhimurium (PDB accession code: 3B60 in magenta) 10 , ADP-bound PglK from C. jejuni (PDB accession code: 5C73 in red) 25 , closed apo-form MsbA from V. cholera (PDB accession code: 3B5X in magenta) 10 or open apo-form MsbA from E. coli (PDB accession code: 3B5W in magenta) 10 (Supplementary Table 1 ). Attempts to superimpose the Mac-NBD on the NBDs of other ABC transporters, such as ABC importers and heterodimeric ABC exporters, were less successful due to differences in the number of helices and the distinct configurations of the NBDs

    Techniques Used: Binding Assay

    Related Articles

    Crystallization Assay:

    Article Title: Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii
    Article Snippet: The purity of MacB was analysed by SDS-PAGE followed by Coomassie Brilliant Blue staining. .. Crystallization Adenosine-5′-(β-thio)-diphosphate of 10 mM (ADPβS, Jena bioscience GmbH, Germany) and 2 mM MgCl2 were added to the purified protein and incubate for overnight on ice before crystallization. .. MacB crystals were grown by the sitting drop vapour diffusion technique at 25 °C.

    Purification:

    Article Title: Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii
    Article Snippet: The purity of MacB was analysed by SDS-PAGE followed by Coomassie Brilliant Blue staining. .. Crystallization Adenosine-5′-(β-thio)-diphosphate of 10 mM (ADPβS, Jena bioscience GmbH, Germany) and 2 mM MgCl2 were added to the purified protein and incubate for overnight on ice before crystallization. .. MacB crystals were grown by the sitting drop vapour diffusion technique at 25 °C.

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    Jena Bioscience adpβs
    Structural comparison between MacB vs. Sav1866 and PglK. Ribbon representation of (left) ADP-bound, outward-open conformation of Sav1866 (blue, PDB accession code: 2HYD) 9 , (middle) ADP bound, outward-occluded conformation of PglK (orange, PDB accession code:5C73) 25 and (right) <t>ADPβS-bound</t> MacB (green), viewed from membrane plane (top) and cytoplasm (bottom). Dotted lines depict the approximate membrane boundaries. Alfa phosphate atoms of the two bound nucleotides are connected by a magenta line showing the interface in each NBD dimer. For ADP-bound PglK, the coordinates of ADP were not deposited in the Protein Data Bank 25 . Outward-facing, V-shaped cavities in the TMDs are depicted as dotted triangles. Elbow helix and connecting TM1, which contribute to the extent of the external opening in each transporter, are coloured in red
    Adpβs, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/adpβs/product/Jena Bioscience
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Image Search Results


    Structural comparison between MacB vs. Sav1866 and PglK. Ribbon representation of (left) ADP-bound, outward-open conformation of Sav1866 (blue, PDB accession code: 2HYD) 9 , (middle) ADP bound, outward-occluded conformation of PglK (orange, PDB accession code:5C73) 25 and (right) ADPβS-bound MacB (green), viewed from membrane plane (top) and cytoplasm (bottom). Dotted lines depict the approximate membrane boundaries. Alfa phosphate atoms of the two bound nucleotides are connected by a magenta line showing the interface in each NBD dimer. For ADP-bound PglK, the coordinates of ADP were not deposited in the Protein Data Bank 25 . Outward-facing, V-shaped cavities in the TMDs are depicted as dotted triangles. Elbow helix and connecting TM1, which contribute to the extent of the external opening in each transporter, are coloured in red

    Journal: Nature Communications

    Article Title: Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii

    doi: 10.1038/s41467-017-01399-2

    Figure Lengend Snippet: Structural comparison between MacB vs. Sav1866 and PglK. Ribbon representation of (left) ADP-bound, outward-open conformation of Sav1866 (blue, PDB accession code: 2HYD) 9 , (middle) ADP bound, outward-occluded conformation of PglK (orange, PDB accession code:5C73) 25 and (right) ADPβS-bound MacB (green), viewed from membrane plane (top) and cytoplasm (bottom). Dotted lines depict the approximate membrane boundaries. Alfa phosphate atoms of the two bound nucleotides are connected by a magenta line showing the interface in each NBD dimer. For ADP-bound PglK, the coordinates of ADP were not deposited in the Protein Data Bank 25 . Outward-facing, V-shaped cavities in the TMDs are depicted as dotted triangles. Elbow helix and connecting TM1, which contribute to the extent of the external opening in each transporter, are coloured in red

    Article Snippet: Crystallization Adenosine-5′-(β-thio)-diphosphate of 10 mM (ADPβS, Jena bioscience GmbH, Germany) and 2 mM MgCl2 were added to the purified protein and incubate for overnight on ice before crystallization.

    Techniques:

    Nucleotide-binding sites in MacB dimer. a NBD dimer and b close-up view of an ATP-binding site interacting with ADPβS. Each monomer in dimeric MacB is coloured in green and red, respectively. Walker A motif in cyan, and carboxy-terminal coupling helix (CH2) in yellow, LSGGQ motif in ABC signature in orange. The difference Fourier map F o– F c (without ADPβS) contoured at 2 σ ( σ is the root mean square electron density of the map) (shown in blue cage) and the anomalous difference Fourier map contoured at 4 σ (shown in red cage) for phosphor and sulphur atoms of bound ADPβS. Bound ADPβS is shown in stick representation in a and b with the positions of the C, N, O, P and S atoms indicated by yellow, blue, red, orange and gold, respectively. The positions of key residues of nucleotide-binding site in b are also shown in stick representation with the position of the C atoms indicated in green. c Structural comparison of NBDs in different nucleotide-bound states. Side view (top row) and top–down view on NBDs (bottom row). Superimposition of the right half of NBD dimers of MacB (green) vs. AMP-PNP-bound Sav1866 from S. aureus (PDB accession code: 2ONJ in blue) 60 , AMP-PNP-bound MsbA from Salmonella typhimurium (PDB accession code: 3B60 in magenta) 10 , ADP-bound PglK from C. jejuni (PDB accession code: 5C73 in red) 25 , closed apo-form MsbA from V. cholera (PDB accession code: 3B5X in magenta) 10 or open apo-form MsbA from E. coli (PDB accession code: 3B5W in magenta) 10 (Supplementary Table 1 ). Attempts to superimpose the Mac-NBD on the NBDs of other ABC transporters, such as ABC importers and heterodimeric ABC exporters, were less successful due to differences in the number of helices and the distinct configurations of the NBDs

    Journal: Nature Communications

    Article Title: Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii

    doi: 10.1038/s41467-017-01399-2

    Figure Lengend Snippet: Nucleotide-binding sites in MacB dimer. a NBD dimer and b close-up view of an ATP-binding site interacting with ADPβS. Each monomer in dimeric MacB is coloured in green and red, respectively. Walker A motif in cyan, and carboxy-terminal coupling helix (CH2) in yellow, LSGGQ motif in ABC signature in orange. The difference Fourier map F o– F c (without ADPβS) contoured at 2 σ ( σ is the root mean square electron density of the map) (shown in blue cage) and the anomalous difference Fourier map contoured at 4 σ (shown in red cage) for phosphor and sulphur atoms of bound ADPβS. Bound ADPβS is shown in stick representation in a and b with the positions of the C, N, O, P and S atoms indicated by yellow, blue, red, orange and gold, respectively. The positions of key residues of nucleotide-binding site in b are also shown in stick representation with the position of the C atoms indicated in green. c Structural comparison of NBDs in different nucleotide-bound states. Side view (top row) and top–down view on NBDs (bottom row). Superimposition of the right half of NBD dimers of MacB (green) vs. AMP-PNP-bound Sav1866 from S. aureus (PDB accession code: 2ONJ in blue) 60 , AMP-PNP-bound MsbA from Salmonella typhimurium (PDB accession code: 3B60 in magenta) 10 , ADP-bound PglK from C. jejuni (PDB accession code: 5C73 in red) 25 , closed apo-form MsbA from V. cholera (PDB accession code: 3B5X in magenta) 10 or open apo-form MsbA from E. coli (PDB accession code: 3B5W in magenta) 10 (Supplementary Table 1 ). Attempts to superimpose the Mac-NBD on the NBDs of other ABC transporters, such as ABC importers and heterodimeric ABC exporters, were less successful due to differences in the number of helices and the distinct configurations of the NBDs

    Article Snippet: Crystallization Adenosine-5′-(β-thio)-diphosphate of 10 mM (ADPβS, Jena bioscience GmbH, Germany) and 2 mM MgCl2 were added to the purified protein and incubate for overnight on ice before crystallization.

    Techniques: Binding Assay