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TitleThree-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer.
Journal, issue, pagesEMBO J, Vol. 22, Issue 23, Page 6175-6181, Year 2003
Publish dateDec 1, 2003
AuthorsIban Ubarretxena-Belandia / Joyce M Baldwin / Shimon Schuldiner / Christopher G Tate /
PubMed AbstractThe 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 ...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 A resolution. The structure of EmrE consists of a bundle of eight transmembrane alpha-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.
External linksEMBO J / PubMed:14633977 / PubMed Central
MethodsEM (electron crystallography)
Resolution7.5 Å
Structure data

EMDB-1087:
Three-dimensional structure of the bacterial multidrug transporter EmrE shows it is an asymmetric homodimer.
Method: EM (electron crystallography) / Resolution: 7.5 Å

Source
  • Escherichia coli (E. coli)

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