Structural highlights
Function
O67159_AQUAE
Publication Abstract from PubMed
Periplasmic adaptor proteins are key components of bacterial tripartite efflux pumps. The 2.85A resolution structure of an MFS (major facilitator superfamily) pump adaptor, Aquifex aeolicus EmrA, shows linearly arranged alpha-helical coiled-coil, lipoyl, and beta-barrel domains, but lacks the fourth membrane-proximal domain shown in other pumps to interact with the inner membrane transporter. The adaptor alpha-hairpin, which binds outer membrane TolC, is exceptionally long at 127A, and the beta-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.
Structure of the periplasmic adaptor protein from a major facilitator superfamily (MFS) multidrug efflux pump.,Hinchliffe P, Greene NP, Paterson NG, Crow A, Hughes C, Koronakis V FEBS Lett. 2014 Jul 1. pii: S0014-5793(14)00519-5. doi:, 10.1016/j.febslet.2014.06.055. PMID:24996185[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hinchliffe P, Greene NP, Paterson NG, Crow A, Hughes C, Koronakis V. Structure of the periplasmic adaptor protein from a major facilitator superfamily (MFS) multidrug efflux pump. FEBS Lett. 2014 Jul 1. pii: S0014-5793(14)00519-5. doi:, 10.1016/j.febslet.2014.06.055. PMID:24996185 doi:http://dx.doi.org/10.1016/j.febslet.2014.06.055
