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Structure of the periplasmic adaptor protein from a major facilitator superfamily (MFS) multidrug efflux pump
Author(s) -
Hinchliffe Philip,
Greene Nicholas P.,
Paterson Neil G.,
Crow Allister,
Hughes Colin,
Koronakis Vassilis
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.06.055
Subject(s) - periplasmic space , major facilitator superfamily , aquifex aeolicus , signal transducing adaptor protein , membrane transport protein , efflux , bacterial outer membrane , inner membrane , microbiology and biotechnology , transport protein , membrane protein , biology , chemistry , biochemistry , transporter , membrane , signal transduction , escherichia coli , mitochondrion , gene
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.