title: ABC transporter architecture and regulatory roles of accessory domains.
abstract: We present an overview of the architecture of ATP-binding cassette (ABC) transporters and dissect the systems in core and accessory domains. The ABC transporter core is formed by the transmembrane domains (TMDs) and the nucleotide binding domains (NBDs) that constitute the actual translocator. The accessory domains include the substrate-binding proteins, that function as high affinity receptors in ABC type uptake systems, and regulatory or catalytic domains that can be fused to either the TMDs or NBDs. The regulatory domains add unique functions to the transporters allowing the systems to act as channel conductance regulators, osmosensors/regulators, and assemble into macromolecular complexes with specific properties.
authors.affiliation: Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
authors.forename: Esther
authors.initials: E
authors.lastname: Biemans-Oldehinkel
authors.forename: Mark K
authors.initials: MK
authors.lastname: Doeven
authors.forename: Bert
authors.initials: B
authors.lastname: Poolman
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000502:physiology*; D002462:Cell Membrane / Q000737:chemistry; D011487:Protein Conformation
chemical_list: D018528:ATP-Binding Cassette Transporters