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

Federici, L., Du, D.J., Walas, F., Matsumura, H., Fernandez-Recio, J., McKeegan, K.S., Borges-Walmsley, M.I., 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 angstrom resolution. Journal of Biological Chemistry, 280, pp. 15307-15314. (doi: 10.1074/jbc.M500401200)

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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 β-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.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:UNSPECIFIED
Authors: Federici, L., Du, D.J., Walas, F., Matsumura, H., Fernandez-Recio, J., McKeegan, K.S., Borges-Walmsley, M.I., Luisi, B.F., and Walmsley, A.R.
College/School:College of Medical Veterinary and Life Sciences
Journal Name:Journal of Biological Chemistry
Journal Abbr.:J Biol Chem.
Publisher:American Society for Biochemistry and Molecular Biology, Inc.
ISSN:0021-9258
ISSN (Online):1083-351X

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