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


Type

Article

Change log

Authors

Hinchliffe, Philip 
Greene, Nicholas P 
Paterson, Neil G 
Hughes, Colin 

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.

Description

Keywords

Adaptor protein, Antibiotic resistance, Crystal structure, Major facilitator superfamily, Multidrug efflux, Amino Acid Sequence, Aquifoliaceae, Bacterial Proteins, Conserved Sequence, Crystallography, X-Ray, Ligands, Membrane Transport Proteins, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Protein Structure, Tertiary

Journal Title

FEBS Lett

Conference Name

Journal ISSN

0014-5793
1873-3468

Volume Title

Publisher

Wiley
Sponsorship
Medical Research Council (G1001104)
Wellcome Trust (101828/Z/13/Z)
This work was supported by grants from the UK Medical Research Council and The Wellcome Trust to C.H. and V.K