PMID:15111102

Citation	Ubarretxena-Belandia, I and Tate, CG (2004) New insights into the structure and oligomeric state of the bacterial multidrug transporter EmrE: an unusual asymmetric homo-dimer. FEBS Lett. 564:234-8
Abstract	EmrE is a small multidrug transporter that contains 110 amino acid residues that form four transmembrane alpha-helices. The three-dimensional structure of EmrE has been determined from two-dimensional crystals by electron cryo-microscopy. EmrE is an asymmetric homo-dimer with one substrate molecule bound in a chamber accessible laterally from one leaflet of the lipid bilayer. Evidence from substrate binding analyses and analytical ultracentrifugation of detergent-solubilised EmrE shows that the minimum functional unit for substrate binding is a dimer. However, it is possible that EmrE exists as a tetramer in vivo and plausible models are suggested based upon analyses of two-dimensional crystals.
Links	PubMed Online version:10.1016/S0014-5793(04)00228-5
Keywords	Antiporters/chemistry; Antiporters/metabolism; Dimerization; Drug Resistance, Microbial; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Lipid Bilayers/chemistry; Lipid Bilayers/metabolism; Membrane Proteins/chemistry; Membrane Proteins/metabolism; Models, Molecular; Protein Structure, Quaternary; Protein Structure, Secondary
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