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

Federici, Luca; Du, Dijun; Walas, Fabien; Matsumura, Hiroyoshi; Fernandez-Recio, Juan; McKeegan, Kenneth S.; Borges-Walmsley, M. Ines; Luisi, Ben F.; Walmsley, Adrian R.

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 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.

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. (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), 15307-15314. https://doi.org/10.1074/jbc.m500401200

• Journal Article Type: Article
• Publication Date: Apr 15, 2005
• Deposit Date: May 14, 2007
• Publicly Available Date: Sep 21, 2016
• Journal: Journal of Biological Chemistry
• Print ISSN: 0021-9258
• Electronic ISSN: 1083-351X
• Publisher: American Society for Biochemistry and Molecular Biology
• Peer Reviewed: Peer Reviewed
• Volume: 280
• Issue: 15
• Pages: 15307-15314
• DOI: https://doi.org/10.1074/jbc.m500401200
• Public URL: https://durham-repository.worktribe.com/output/1587998