title: Mechanism of Action of ABC Importers: Conservation, Divergence, and Physiological Adaptations.
abstract: The past decade has seen a remarkable surge in structural characterization of ATP binding cassette (ABC) transporters, which have spurred a more focused functional analysis of these elaborate molecular machines. As a result, it has become increasingly apparent that there is a substantial degree of mechanistic variation between ABC transporters that function as importers, which correlates with their physiological roles. Here, we summarize recent advances in ABC importers' structure-function studies and provide an explanation as to the origin of the different mechanisms of action.
authors.affiliation: Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, 31096 Haifa, Israel. Electronic address: lewinson@tx.technion.ac.il.
authors.forename: Oded
authors.initials: O
authors.lastname: Lewinson
authors.affiliation: Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, 31096 Haifa, Israel.
authors.forename: Nurit
authors.initials: N
authors.lastname: Livnat-Levanon
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000235:genetics / Q000378:metabolism*; D000222:Adaptation, Physiological; D000255:Adenosine Triphosphate / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation
chemical_list: D018528:ATP-Binding Cassette Transporters; D000255:Adenosine Triphosphate
keywords: ABC transporter; ATP hydrolysis; membrane protein; structure–function; substrate-binding protein