Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer

Iban Ubarretxena-Belandia, Joyce M. Baldwin, Shimon Schuldiner, Christopher G. Tate*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

175 Scopus citations

Abstract

The small multidrug resistance family of transporters is widespread in bacteria and is responsible for bacterial resistance to toxic aromatic cations by proton-linked efflux. We have determined the three-dimensional (3D) structure of the Escherichia coli multidrug transporter EmrE by electron cryomicroscopy of 2D crystals, including data to 7.0 Å resolution. The structure of EmrE consists of a bundle of eight transmembrane α-helices with one substrate molecule bound near the centre. The substrate binding chamber is formed from six helices and is accessible both from the aqueous phase and laterally from the lipid bilayer. The most remarkable feature of the structure of EmrE is that it is an asymmetric homodimer. The possible arrangement of the two polypeptides in the EmrE dimer is discussed based on the 3D density map.

Original languageEnglish
Pages (from-to)6175-6181
Number of pages7
JournalEMBO Journal
Volume22
Issue number23
DOIs
StatePublished - 1 Dec 2003

Keywords

  • Asymmetry
  • Electron crystallography
  • Membrane protein
  • Multidrug
  • Structure

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