title: Structural diversity of ABC transporters.
abstract: ATP-binding cassette (ABC) transporters form a large superfamily of ATP-dependent protein complexes that mediate transport of a vast array of substrates across membranes. The 14 currently available structures of ABC transporters have greatly advanced insight into the transport mechanism and revealed a tremendous structural diversity. Whereas the domains that hydrolyze ATP are structurally related in all ABC transporters, the membrane-embedded domains, where the substrates are translocated, adopt four different unrelated folds. Here, we review the structural characteristics of ABC transporters and discuss the implications of this structural diversity for mechanistic diversity.
authors.affiliation: Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, Netherlands.
authors.forename: Josy
authors.initials: J
authors.lastname: ter Beek
authors.forename: Albert
authors.initials: A
authors.lastname: Guskov
authors.forename: Dirk Jan
authors.initials: DJ
authors.lastname: Slotboom
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D003460:Crystallization; D006801:Humans; D011485:Protein Binding / Q000502:physiology; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D018528:ATP-Binding Cassette Transporters