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X-ray structure of emre supports dual topology model

Academic Article
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Overview

authors

  • Chen, Y. J.
  • Pornillos, O.
  • Lieu, S.
  • Ma, C.
  • Chen, A. P.
  • Chang, Geoffrey

publication date

  • November 2007

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • EmrE, a multidrug transporter from Escherichia coli, functions as a homodimer of a small four-transmembrane protein. The membrane insertion topology of the two monomers is controversial. Although the EmrE protein was reported to have a unique orientation in the membrane, models based on electron microscopy and now defunct x-ray structures, as well as recent biochemical studies, posit an antiparallel dimer. We have now reanalyzed our x-ray data on EmrE. The corrected structures in complex with a transport substrate are highly similar to the electron microscopy structure. The first three transmembrane helices from each monomer surround the substrate binding chamber, whereas the fourth helices participate only in dimer formation. Selenomethionine markers clearly indicate an antiparallel orientation for the monomers, supporting a "dual topology" model.

subject areas

  • Amino Acid Sequence
  • Antiporters
  • Crystallography, X-Ray
  • Escherichia coli Proteins
  • Fluorescence Polarization
  • Models, Molecular
  • Molecular Sequence Data
  • Onium Compounds
  • Organophosphorus Compounds
  • Protein Conformation
  • Recombinant Proteins
  • Selenomethionine
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Research

keywords

  • SMR family
  • membrane protein structure
  • multidrug transport
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Identity

PubMed Central ID

  • PMC2141897

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0709387104

PubMed ID

  • 18024586
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Additional Document Info

start page

  • 18999

end page

  • 19004

volume

  • 104

issue

  • 48

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