1g6h: Difference between revisions
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|PDB= 1g6h |SIZE=350|CAPTION= <scene name='initialview01'>1g6h</scene>, resolution 1.60Å | |PDB= 1g6h |SIZE=350|CAPTION= <scene name='initialview01'>1g6h</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MMC:METHYL+MERCURY+ION'>MMC</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g6h OCA], [http://www.ebi.ac.uk/pdbsum/1g6h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g6h RCSB]</span> | |||
}} | }} | ||
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[[Category: Thomas, P J.]] | [[Category: Thomas, P J.]] | ||
[[Category: Yuan, Y R.]] | [[Category: Yuan, Y R.]] | ||
[[Category: abc specific-beta-strand domain alpha-helix domain]] | [[Category: abc specific-beta-strand domain alpha-helix domain]] | ||
[[Category: beta-core domain]] | [[Category: beta-core domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:37:36 2008'' | ||
Revision as of 20:37, 30 March 2008
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| , resolution 1.60Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE ADP CONFORMATION OF MJ1267, AN ATP-BINDING CASSETTE OF AN ABC TRANSPORTER
OverviewOverview
BACKGROUND: ATP binding cassette (ABC) transporters are ubiquitously distributed transmembrane solute pumps that play a causative role in numerous diseases. Previous structures have defined the fold of the ABC and established the flexibility of its alpha-helical subdomain. But the nature of the mechanical changes that occur at each step of the chemical ATPase cycle have not been defined. RESULTS: Crystal structures were determined of the MJ1267 ABC from Methanococcus jannaschii in Mg-ADP-bound and nucleotide-free forms. Comparison of these structures reveals an induced-fit effect at the active site likely to be a consequence of nucleotide binding. In the Mg-ADP-bound structure, the loop following the Walker B moves toward the Walker A (P-loop) coupled to backbone conformational changes in the intervening "H-loop", which contains an invariant histidine. These changes affect the region believed to mediate intercassette interaction in the ABC transporter complex. Comparison of the Mg-ADP-bound structure of MJ1267 to the ATP-bound structure of HisP suggests that an outward rotation of the alpha-helical subdomain is coupled to the loss of a molecular contact between the gamma-phosphate of ATP and an invariant glutamine in a segment connecting this subdomain to the core of the cassette. CONCLUSIONS: The induced-fit effect and rotation of the alpha-helical subdomain may play a role in controlling the nucleotide-dependent change in cassette-cassette interaction affinity believed to represent the power-stroke of ABC transporters. Outward rotation of the alpha-helical subdomain also likely facilitates Mg-ADP release after hydrolysis. The MJ1267 structures therefore define features of the nucleotide-dependent conformational changes that drive transmembrane transport in ABC transporters.
About this StructureAbout this Structure
1G6H is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter., Karpowich N, Martsinkevich O, Millen L, Yuan YR, Dai PL, MacVey K, Thomas PJ, Hunt JF, Structure. 2001 Jul 3;9(7):571-86. PMID:11470432
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