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Structure of a cation-bound multidrug and toxic compound extrusion transporter

Academic Article
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Overview

authors

  • He, X. A.
  • Szewczyk, P.
  • Karyakin, A.
  • Evin, M.
  • Hong, W. X.
  • Zhang, Qinghai
  • Chang, Geoffrey

publication date

  • October 2010

journal

  • Nature  Journal

abstract

  • Transporter proteins from the MATE (multidrug and toxic compound extrusion) family are vital in metabolite transport in plants, directly affecting crop yields worldwide. MATE transporters also mediate multiple-drug resistance (MDR) in bacteria and mammals, modulating the efficacy of many pharmaceutical drugs used in the treatment of a variety of diseases. MATE transporters couple substrate transport to electrochemical gradients and are the only remaining class of MDR transporters whose structure has not been determined. Here we report the X-ray structure of the MATE transporter NorM from Vibrio cholerae determined to 3.65 Å, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other known MDR transporter. We also report a cation-binding site in close proximity to residues previously deemed critical for transport. This conformation probably represents a stage of the transport cycle with high affinity for monovalent cations and low affinity for substrates.

subject areas

  • Antiporters
  • Bacterial Proteins
  • Binding Sites
  • Cations
  • Crystallography, X-Ray
  • Cysteine
  • Ion Transport
  • Models, Molecular
  • Protein Conformation
  • Reproducibility of Results
  • Static Electricity
  • Substrate Specificity
  • Vibrio cholerae
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Identity

PubMed Central ID

  • PMC3152480

International Standard Serial Number (ISSN)

  • 0028-0836

Digital Object Identifier (DOI)

  • 10.1038/nature09408

PubMed ID

  • 20861838
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Additional Document Info

start page

  • 991

end page

  • 994

volume

  • 467

issue

  • 7318

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