Structure and mechanism of ATP-binding cassette transporters

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 whi...

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Bibliographic Details
Published in:Philosophical transactions of the Royal Society of London. Series B. Biological sciences 2009-01, Vol.364 (1514), p.239-245
Main Author: Locher, Kaspar P
Format: Article
Language:English
Subjects:
Architecture
ATP binding cassette transporters
ATP-binding cassette (ABC) transporter
Binding sites
Biochemistry
Carrier proteins
Crystal Structure
Exporters
Hydrolysis
Importers
Mechanism
Membrane Transport Proteins
Review
Reviews
Structure-Function Relationship
Topology
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Summary: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.
ISSN:0962-8436
1471-2970
DOI:10.1098/rstb.2008.0125