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

Federici, L. and Du, D. and Walas, F. and Matsumura, H. and Fernandez-Recio, J. and McKeegan, K. S. and Borges-Walmsley, M. I. and Luisi, B. F. and Walmsley, A. R. (2005) 'The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 Å resolution.', Journal of biological chemistry., 280 (15). pp. 15307-15314.


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 Å 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 -barrel domain in a fashion that may mimic proteinlipopolysaccharide 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.

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Publisher statement:This research was originally published in Journal of Biological Chemistry. 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 Å Resolution. Journal of Biological Chemistry. 2005. 280: 15307-15314. © the American Society for Biochemistry and Molecular Biology
Record Created:14 May 2007
Last Modified:29 Aug 2017 14:54

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