3D structure of AcrB: the archetypal multidrug efflux transporter of Escherichia coli likely captures substrates from periplasm.
Recent advances in structural biology have extended our understanding of the multiple drug efflux complex, AcrAB-TolC, of Escherichia coli. This tripartite complex and its homologs are the major mechanisms that give most Gram-negative bacteria their characteristic intrinsic resistance to a variety of lipophilic drugs, dyes, and detergents. Most recently, the structure of the transporter AcrB was elucidated at high resolution [Nature 419(2002)587]. It is a particularly significant achievement since integral membrane proteins are notoriously elusive structures for crystallography. The striking features of this trimeric pump, such as the presence of potential substrate-binding sites in the periplasmic domain and the possibility of direct interaction with the end of TolC tunnel, refine our understanding of the mode of action of this tripartite efflux transport complex.
Elkins
Christopher A
CA
Department of Molecular and Cell Biology, 426, Barker Hall, University of California, Berkeley, CA 94720-3202, USA.
Nikaido
Hiroshi
H
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry* / Q000502:physiology; D018360:Crystallography, X-Ray; D024901:Drug Resistance, Multiple, Bacterial; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000502:physiology; D008565:Membrane Proteins / Q000737:chemistry* / Q000502:physiology; D026901:Membrane Transport Proteins; D008958:Models, Molecular; D027425:ATP-Binding Cassette, Sub-Family C Proteins; D019897:Periplasm / Q000502:physiology*; D020836:Protein Structure, Quaternary
D001425:Bacterial Outer Membrane Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D026901:Membrane Transport Proteins; D027425:ATP-Binding Cassette, Sub-Family C Proteins; C083496:AcrB protein, E coli; C073126:tolC protein, E coli