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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred


SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

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1437-4315
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Structural and functional aspects of the multidrug efflux pump AcrB

Thomas Eicher1 / Lorenz Brandstätter1 / Klaas M. Pos2

1Institute of Physiology and Zurich Center for Integrative Human Physiology (ZIHP), University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland

2Cluster of Excellence Frankfurt – Macromolecular Complexes and Institute of Biochemistry, Goethe University Frankfurt, Max-von-Laue-Str. 9, D-60438 Frankfurt/Main, Germany

Corresponding author

Citation Information: Biological Chemistry. Volume 390, Issue 8, Pages 693–699, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2009.090, May 2009

Publication History

Received:
2009-03-01
Accepted:
2009-04-29
Published Online:
2009-05-20

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.

Keywords: AcrB; alternate access transport mechanism; antibiotic resistance; binding change mechanism; drug transport; membrane protein structure; multiple drug efflux pump

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