Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirochete Borrelia burgdorferi. Issue 18 (10th July 2013)

• Record Type: Journal Article
• Authors: Greene, Nicholas P.; Hinchliffe, Philip; Crow, Allister; Ababou, Abdessamad; Hughes, Colin; Koronakis, Vassilis
• Is Part Of: FEBS letters. Volume 587:Issue 18(2013)
• Page Start: 2984
• Page End: 2988
• Publication Date: 2013-07-10
• Subjects: MDR -- multidrug resistance -- IM -- inner membrane -- OM -- outer membrane -- MP -- membrane proximal -- RMSDs -- root mean square deviations -- HME -- heavy metal efflux -- MD -- molecular dynamics -- Antibiotic resistance -- Multidrug efflux -- Adaptor protein -- Crystal structure; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.06.056
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract : Periplasmic adaptors are essential to tripartite drug efflux pump assembly. We present the structure of the periplasmic adaptor BesA from Borrelia burgdorferi . BesA lacks the α‐hairpin shown to underpin exit duct recruitment and pump assembly. Recruitment of the TolC exit duct must be different in this pump. The BesA structure has implications for proposed models of pump assembly.