Format

Send to

Choose Destination
See comment in PubMed Commons below
Philos Trans R Soc Lond B Biol Sci. 2009 Jan 27;364(1514):239-45. doi: 10.1098/rstb.2008.0125.

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

Author information

  • 1Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland. locher@mol.biol.ethz.ch

Abstract

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.

PMID:
18957379
PMCID:
PMC2674090
DOI:
10.1098/rstb.2008.0125
[PubMed - indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Support Center