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Review Structure and mechanism of ATP-binding cassette transporters Locher KPPhilos Trans R Soc Lond B Biol Sci 2009[Jan]; 364 (1514): 239-45ATP-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.|ATP-Binding Cassette Transporters/*chemistry/classification/*metabolism[MESH]|Models, Molecular[MESH]|Protein Conformation[MESH]|Protein Structure, Tertiary[MESH] |
