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

DOI: 10.1016/j.febslet.2013.06.056 DOI Help

Authors: Nicholas Greene (University of Cambridge) , Philip Hinchliffe (University of Cambridge) , Allister Crow (University of Cambridge) , Abdessamad Ababou (University of Cambridge) , Colin Hughes (University of Cambridge) , Vassilis Koronakis (University of Cambridge)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Febs Letters

State: Published (Approved)
Published: July 2013

Open Access Open Access

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 Keywords: Antibiotic Resistance; Multidrug Efflux; Adaptor Protein; Crystal Structure

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials, Medicine

Instruments: I02-Macromolecular Crystallography

Other Facilities: ID29 at ESRF

Added On: 12/08/2013 15:24

FEBS Letters - 2013 - Greene - Structure of an atypical periplasmic adaptor from a multidrug efflux pump of the spirochete.pdf

Discipline Tags:

Pathogens Antibiotic Resistance Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)