The crystal structure of the outer membrane protein VceC from the bacterial pathogen Vibrio cholerae at 1.8 Å resolution (2005)
Journal Article
Federici, L., Du, D., Walas, F., Matsumura, H., Fernandez-Recio, J., McKeegan, K., …Walmsley, A. (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

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

A kinetic model for the action of a resistance efflux pump (2001)
Journal Article
Walmsley, A., Zhou, T., Borges-Walmsley, M., & Rosen, B. (2001). A kinetic model for the action of a resistance efflux pump. Journal of Biological Chemistry, 276(9), 6378-6391. https://doi.org/10.1074/jbc.m008105200

ArsA is the catalytic subunit of the arsenical pump, coupling ATP hydrolysis to the efflux of arsenicals through the ArsB membrane protein. It is a paradigm for understanding the structure-function of the nucleotide binding domains (NBD) of medically... Read More about A kinetic model for the action of a resistance efflux pump.