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Structure of the periplasmic adaptor protein from a major facilitator superfamily (MFS) multidrug efflux pump

DOI: 10.1016/j.febslet.2014.06.055 DOI Help
PMID: 24996185 PMID Help

Authors: Philip Hinchliffe (University of Cambridge) , Nicholas P. Greene (University of Cambridge) , Neil G. Paterson (Diamond Light Source) , Allister Crow (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 , VOL 588 (17) , PAGES 3147 - 3153

State: Published (Approved)
Published: August 2014

Open Access Open Access

Abstract: Periplasmic adaptor proteins are key components of bacterial tripartite efflux pumps. The 2.85 Å resolution structure of an MFS (major facilitator superfamily) pump adaptor, Aquifex aeolicus EmrA, shows linearly arranged alpha-helical coiled-coil, lipoyl, and beta-barrel domains, but lacks the fourth membrane-proximal domain shown in other pumps to interact with the inner membrane transporter. The adaptor alpha-hairpin, which binds outer membrane TolC, is exceptionally long at 127 Å, and the beta-barrel contains a conserved disordered loop. The structure extends the view of adaptors as flexible, modular components that mediate diverse pump assembly, and suggests that in MFS tripartite pumps a hexamer of adaptors could provide a periplasmic seal.

Journal Keywords: Aquifoliaceae; Bacterial; Conserved; Crystallography; X-Ray; Ligands; Membrane; Models; Molecular; Protein; Secondary; Protein; Tertiary

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography

Added On: 13/02/2015 20:24

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