Journal
FEBS LETTERS
Volume 587, Issue 18, Pages 2984-2988Publisher
WILEY
DOI: 10.1016/j.febslet.2013.06.056
Keywords
Antibiotic resistance; Multidrug efflux; Adaptor protein; Crystal structure
Funding
- UK Medical Research Council
- Wellcome Trust
- MRC [G1001104] Funding Source: UKRI
- Medical Research Council [G1001104] Funding Source: researchfish
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Periplasmic adaptor proteins are essential components of bacterial tripartite multidrug efflux pumps. Here we report the 2.35 angstrom resolution crystal structure of the BesA adaptor from the spirochete Borrelia burgdorferi solved using selenomethionine derivatized protein. BesA shows the archetypal linear, flexible, multi-domain architecture evident among proteobacteria and retains the lipoyl, beta-barrel and membrane-proximal domains that interact with the periplasmic domains of the inner membrane transporter. However, it lacks the alpha-hairpin domain shown to establish extensive coiled-coil interactions with the periplasmic entrance helices of the outer membrane-anchored TolC exit duct. This has implications for the modelling of assembled tripartite efflux pumps. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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