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Review. Structure and mechanism of ATP-binding cassette transporters.

  • Locher KP Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland. locher@mol.biol.ethz.ch
  • 2008-10-30
Published in:
  • Philosophical transactions of the Royal Society of London. Series B, Biological sciences. - 2009
ATP-Binding Cassette Transporters
Models, Molecular
Protein Conformation
Protein Structure, Tertiary
English ATP-binding cassette (ABC) transporters constitute a large superfamily of integral membrane proteins that includes both importers and exporters. In recent years, several structures of complete ABC transporters have been determined by X-ray crystallography. These structures suggest a mechanism by which binding and hydrolysis of ATP by the cytoplasmic, nucleotide-binding domains control the conformation of the transmembrane domains and therefore which side of the membrane the translocation pathway is exposed to. A basic, conserved two-state mechanism can explain active transport of both ABC importers and ABC exporters, but various questions remain unresolved. In this article, I will review some of the crystal structures and the mechanistic insight gained from them. Future challenges for a better understanding of the mechanism of ABC transporters will be outlined.
Language
  • English
Open access status
green
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https://folia.unifr.ch/global/documents/229308
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