Mechanistic diversity in ATP-binding cassette (ABC) transporters.
ABC transporters catalyze transport reactions, such as the high-affinity uptake of micronutrients into bacteria and the export of cytotoxic compounds from mammalian cells. Crystal structures of ABC domains and full transporters have provided a framework for formulating reaction mechanisms of ATP-driven substrate transport, but recent studies have suggested remarkable mechanistic diversity within this protein family. This review evaluates the differing mechanistic proposals and outlines future directions for the exploration of ABC-transporter-catalyzed reactions.
Institute of Molecular Biology and Biophysics, Department of Biology, ETH Zurich, Zurich, Switzerland.
Kaspar P
KP
Locher
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000145:classification* / Q000235:genetics / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000737:chemistry* / Q000378:metabolism; D000818:Animals; D001419:Bacteria / Q000737:chemistry; D001692:Biological Transport; D020134:Catalytic Domain; D015870:Gene Expression; D006801:Humans; D006868:Hydrolysis; D008958:Models, Molecular; D011485:Protein Binding; D000072417:Protein Domains; D017510:Protein Folding; D017433:Protein Structure, Secondary
D018528:ATP-Binding Cassette Transporters; D000255:Adenosine Triphosphate