title: Structural and functional aspects of the multidrug efflux pump AcrB.
abstract: The tripartite efflux system AcrA/AcrB/TolC is the main pump in Escherichia coli for the efflux of multiple antibiotics, dyes, bile salts and detergents. The inner membrane component AcrB is central to substrate recognition and energy transduction and acts as a proton/drug antiporter. Recent structural studies show that homotrimeric AcrB can adopt different monomer conformations representing consecutive states in an allosteric functional rotation transport cycle. The conformational changes create an alternate access drug transport tunnel including a hydrophobic substrate binding pocket in one of the cycle intermediates.
authors.affiliation: Institute of Physiology and Zurich Center for Integrative Human Physiology (ZIHP), University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland.
authors.forename: Thomas
authors.initials: T
authors.lastname: Eicher
authors.forename: Lorenz
authors.initials: L
authors.lastname: Brandstätter
authors.forename: Klaas M
authors.initials: KM
authors.lastname: Pos
mesh_terms: D024901:Drug Resistance, Multiple, Bacterial; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008958:Models, Molecular; D027425:ATP-Binding Cassette, Sub-Family C Proteins / Q000737:chemistry*; D013379:Substrate Specificity
chemical_list: D029968:Escherichia coli Proteins; D027425:ATP-Binding Cassette, Sub-Family C Proteins; C083496:AcrB protein, E coli