Structural highlights
Function
O51166_BORBU
Publication Abstract from PubMed
Periplasmic adaptor proteins are essential components of bacterial tripartite multidrug efflux pumps. Here we report the 2.35A 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, beta-barrel and membrane-proximal domains that interact with the periplasmic domains of the inner membrane transporter. However, it lacks the alpha-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.
Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirochete Borrelia burgdorferi.,Greene NP, Hinchliffe P, Crow A, Ababou A, Hughes C, Koronakis V FEBS Lett. 2013 Jul 9. pii: S0014-5793(13)00520-6. doi:, 10.1016/j.febslet.2013.06.056. PMID:23851070[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Greene NP, Hinchliffe P, Crow A, Ababou A, Hughes C, Koronakis V. Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirochete Borrelia burgdorferi. FEBS Lett. 2013 Jul 9. pii: S0014-5793(13)00520-6. doi:, 10.1016/j.febslet.2013.06.056. PMID:23851070 doi:10.1016/j.febslet.2013.06.056
