The projection structure of EmrE, a proton-linked multidrug transporter from Escherichia coli, at 7 Å

Christopher G. Tate*, Edmund R.S. Kunji, Mario Lebendiker, Shimon Schuldiner

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

105 Scopus citations

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 Å resolution. The projection map shows an asymmetric EmrE dimer with overall dimensions ∼31 x 40 Å, 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.

Original languageEnglish
Pages (from-to)77-81
Number of pages5
JournalEMBO Journal
Volume20
Issue number1-2
DOIs
StatePublished - 15 Jan 2001

Keywords

  • Ion-coupled transport
  • Membrane proteins
  • Multidrug resistance
  • Structure

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