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Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirochete Borrelia burgdorferi
Author(s) -
Greene Nicholas P.,
Hinchliffe Philip,
Crow Allister,
Ababou Abdessamad,
Hughes Colin,
Koronakis Vassilis
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.06.056
Subject(s) - periplasmic space , borrelia burgdorferi , efflux , bacterial outer membrane , signal transducing adaptor protein , biology , membrane transport protein , biophysics , inner membrane , microbiology and biotechnology , membrane protein , chemistry , biochemistry , membrane , signal transduction , genetics , escherichia coli , antibody , gene
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.