1yc9
From Proteopedia
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|PDB= 1yc9 |SIZE=350|CAPTION= <scene name='initialview01'>1yc9</scene>, resolution 1.80Å | |PDB= 1yc9 |SIZE=350|CAPTION= <scene name='initialview01'>1yc9</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene> | + | |LIGAND= <scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yc9 OCA], [http://www.ebi.ac.uk/pdbsum/1yc9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yc9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Walas, F.]] | [[Category: Walas, F.]] | ||
[[Category: Walmsley, A R.]] | [[Category: Walmsley, A R.]] | ||
| - | [[Category: BOG]] | ||
| - | [[Category: HG]] | ||
[[Category: multidrug resistance]] | [[Category: multidrug resistance]] | ||
[[Category: outer membrane protein]] | [[Category: outer membrane protein]] | ||
[[Category: vibrio cholerae]] | [[Category: vibrio cholerae]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:02:34 2008'' |
Revision as of 22:02, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 resolution
Overview
Multidrug resistance in Gram-negative bacteria arises in part from the activities of tripartite drug efflux pumps. In the pathogen Vibrio cholerae, one such pump comprises the inner membrane proton antiporter VceB, the periplasmic adaptor VceA, and the outer membrane channel VceC. Here, we report the crystal structure of VceC at 1.8 A resolution. The trimeric VceC is organized in the crystal lattice within laminar arrays that resemble membranes. A well resolved detergent molecule within this array interacts with the transmembrane beta-barrel domain in a fashion that may mimic protein-lipopolysaccharide contacts. Our analyses of the external surfaces of VceC and other channel proteins suggest that different classes of efflux pumps have distinct architectures. We discuss the implications of these findings for mechanisms of drug and protein export.
About this Structure
1YC9 is a Single protein structure of sequence from Vibrio cholerae. Full crystallographic information is available from OCA.
Reference
The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 A resolution., Federici L, Du D, Walas F, Matsumura H, Fernandez-Recio J, McKeegan KS, Borges-Walmsley MI, Luisi BF, Walmsley AR, J Biol Chem. 2005 Apr 15;280(15):15307-14. Epub 2005 Jan 31. PMID:15684414
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