Abstract
EmrE belongs to a family of eubacterial multidrug transporters that confer resistance to a wide variety of toxins by coupling the influx of protons to toxin extrusion. EmrE was purified and crystallized in two dimensions by reconstitution with dimyristoylphosphatidylcholine into lipid bilayers. Images of frozen hydrated crystals were collected by cryo-electron microscopy and a projection structure of EmrE was calculated to 7 A resolution. The projection map shows an asymmetric EmrE dimer with overall dimensions approximately 31 x 40 A, comprising an arc of highly tilted helices separating two helices nearly perpendicular to the membrane from another two helices, one tilted and the other nearly perpendicular. There is no obvious 2-fold symmetry axis perpendicular to the membrane within the dimer, suggesting that the monomers may have different structures in the functional unit.
MeSH Terms
Antiporters/chemistry,ultrastructure
Bacterial Proteins/chemistry,ultrastructure
Cryoelectron Microscopy
Crystallography, X-Ray/methods
Dimerization
Dimyristoylphosphatidylcholine
Drug Resistance, Multiple
Escherichia coli/physiology
Escherichia coli Proteins
Lipid Bilayers
Membrane Proteins/chemistry,ultrastructure
Protein Structure, Secondary
Recombinant Proteins/chemistry,ultrastructure
Chemicals
Antiporters
Bacterial Proteins
Escherichia coli Proteins
Lipid Bilayers
Membrane Proteins
Recombinant Proteins
EmrE protein, E coli
Dimyristoylphosphatidylcholine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Tate C G
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, MRC Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK.
Kunji E R
Lebendiker M
Schuldiner S
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