1YC9

The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 resolution

Summary for 1YC9

• Entry DOI: 10.2210/pdb1yc9/pdb
• Descriptor: multidrug resistance protein, octyl beta-D-glucopyranoside, MERCURY (II) ION, ... (4 entities in total)
• Functional Keywords: vibrio cholerae, outer membrane protein, multidrug resistance, membrane protein
• Biological source: Vibrio cholerae
• Total number of polymer chains: 1
• Total formula weight: 48378.37

Authors

Federici, L.,Du, D.,Walas, F.,Matsumura, H.,Fernandez-Recio, J.,McKeegan, K.S.,Borges-Walmsley, M.I.,Luisi, B.F.,Walmsley, A.R. (deposition date: 2004-12-22, release date: 2005-03-01, Last modification date: 2024-05-29)

Primary citation

Federici, L.,Du, D.,Walas, F.,Matsumura, H.,Fernandez-Recio, J.,McKeegan, K.S.,Borges-Walmsley, M.I.,Luisi, B.F.,Walmsley, A.R.
The crystal structure of the outer membrane protein VCEC from the bacterial pathogen vibrio cholerae at 1.8 A resolution
J.Biol.Chem., 280:15307-15314, 2005

PubMed Abstract: 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.

PubMed: 15684414
DOI: 10.1074/jbc.M500401200

Experimental method

X-RAY DIFFRACTION (1.8 Å)