title: ABC transporter architecture and mechanism: implications from the crystal structures of BtuCD and BtuF.
abstract: ABC transporters are ubiquitous membrane proteins that facilitate unidirectional substrate translocation across the lipid bilayer. Over the past five years, new crystal structures have advanced our understanding of how ABC transporters couple adenosine triphosphate (ATP) hydrolysis to substrate transport. In the following, we will briefly review the results of these structural investigations and outline their mechanistic implications.
authors.affiliation: Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Zürich, CH-8093 Zürich, Switzerland. locher@mol.biol.ethz.ch
authors.forename: Kaspar P
authors.initials: KP
authors.lastname: Locher
authors.forename: Elizabeth
authors.initials: E
authors.lastname: Borths
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D018360:Crystallography, X-Ray; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D033902:Periplasmic Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D018528:ATP-Binding Cassette Transporters; C050021:BtuC peptide, E coli; D029968:Escherichia coli Proteins; D033902:Periplasmic Binding Proteins; C446048:btuF protein, E coli; D000255:Adenosine Triphosphate