Greene, Nicholas P., Hinchliffe, Philip, Crow, Allister, Ababou, Abdessamad, Hughes, Colin and Koronakis, Vassilis (2013) Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirocheteBorrelia burgdorferi. FEBS Letters, 587 (18). pp. 2984-2988. doi:10.1016/j.febslet.2013.06.056 ISSN 0014-5793.

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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.

Item Type:	Journal Article
Divisions:	Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Journal or Publication Title:	FEBS Letters
Publisher:	Elsevier BV
ISSN:	0014-5793
Official Date:	2013
Dates:	Date Event 2013 Published 1 September 2013 Accepted
Volume:	587
Number:	18
Page Range:	pp. 2984-2988
DOI:	10.1016/j.febslet.2013.06.056
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Open Access (Creative Commons)

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