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

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Hinchliffe, Philip, Greene, Nicholas P., Paterson, Neil G., Crow, Allister, Hughes, Colin and Koronakis, Vassilis (2014) Structure of the periplasmic adaptor protein from a major facilitator superfamily (MFS) multidrug efflux pump. FEBS Letters, 588 (17). pp. 3147-3153. doi:10.1016/j.febslet.2014.06.055 ISSN 0014-5793.

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Official URL: http://dx.doi.org/10.1016/j.febslet.2014.06.055

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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 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 127 Å, 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.

Item Type: Journal Article
Divisions: Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- )
Journal or Publication Title: FEBS Letters
Publisher: Elsevier BV
ISSN: 0014-5793
Official Date: 24 August 2014
Dates:
DateEvent
24 August 2014Published
23 June 2014Accepted
Volume: 588
Number: 17
Page Range: pp. 3147-3153
DOI: 10.1016/j.febslet.2014.06.055
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Restricted or Subscription Access

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