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 Lettjournal_title
FEBS lettersauthors
Greene NP,Hinchliffe P,Crow A,Ababou A,Hughes C,Koronakis Vdoi
10.1016/j.febslet.2013.06.056subject
Has Abstractpub_date
2013-09-17 00:00:00pages
2984-8issue
18eissn
0014-5793issn
1873-3468pii
S0014-5793(13)00520-6journal_volume
587pub_type
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