Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirochete Borrelia burgdorferi |
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Authors: | Nicholas P. Greene Philip Hinchliffe Allister Crow Abdessamad AbabouColin Hughes Vassilis Koronakis |
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Affiliation: | Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK |
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Abstract: | Periplasmic adaptor proteins are essential components of bacterial tripartite multidrug efflux pumps. Here we report the 2.35 Å 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, β-barrel and membrane-proximal domains that interact with the periplasmic domains of the inner membrane transporter. However, it lacks the α-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. |
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Keywords: | MDR, multidrug resistance IM, inner membrane OM, outer membrane MP, membrane proximal RMSDs, root mean square deviations HME, heavy metal efflux MD, molecular dynamics |
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