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Wiley, FEBS Letters, 17(588), p. 3147-3153, 2014

DOI: 10.1016/j.febslet.2014.06.055

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

Journal article published in 2014 by Philip Hinchliffe ORCID, Nicholas P. Greene ORCID, Neil G. Paterson, Allister Crow ORCID, Colin Hughes, Vassilis Koronakis ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Periplasmic adaptor proteins are key components of bacterial tripartite efflux pumps. The 2.85Å resolution structure of an MFS (major facilitator superfamily) pump adaptor, Aquifex aeolicus EmrA, shows linearly arranged α-helical coiled-coil, lipoyl, and β-barrel domains, but lacks the fourth membrane-proximal domain shown in other pumps to interact with the inner membrane transporter. The adaptor α-hairpin, which binds outer membrane TolC, is exceptionally long at 127Å, and the β-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.