Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirochete Borrelia burgdorferi.

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Greene NP,Hinchliffe P,Crow A,Ababou A,Hughes C,Koronakis V

doi

10.1016/j.febslet.2013.06.056

subject

Has Abstract

pub_date

2013-09-17 00:00:00

pages

2984-8

issue

18

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(13)00520-6

journal_volume

587

pub_type

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