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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
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 | ||||||
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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: |
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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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