Journal
PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES
Volume 364, Issue 1514, Pages 239-245Publisher
ROYAL SOC
DOI: 10.1098/rstb.2008.0125
Keywords
ATP-binding cassette (ABC) transporter; crystal structure; membrane transport proteins; mechanism; structure-function relationship
Categories
Funding
- Swiss National Science Foundation (SNSF)
- Roche Research Fund (RRF)
- National Center for Excellence in Research (NCCR) Structural Biology, Zurich
- Swiss Cancer League Oncosuisse
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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.
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