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Structural and functional aspects of the multidrug efflux pump AcrB


Eicher, Thomas; Brandstätter, Lorenz; Pos, Klaas M (2009). Structural and functional aspects of the multidrug efflux pump AcrB. Biological Chemistry, 390(8):693-699.

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

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

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:National licences > 142-005
Dewey Decimal Classification:540 Chemistry
Scopus Subject Areas:Life Sciences > Biochemistry
Life Sciences > Molecular Biology
Life Sciences > Clinical Biochemistry
Uncontrolled Keywords:AcrB; alternate access transport mechanism; antibiotic resistance; binding change mechanism; drug transport; membrane protein structure; multiple drug efflux pump
Language:English
Date:1 January 2009
Deposited On:06 Nov 2018 16:30
Last Modified:26 Jan 2022 17:52
Publisher:De Gruyter
ISSN:1431-6730
OA Status:Green
Publisher DOI:https://doi.org/10.1515/bc.2009.090
  • Content: Published Version
  • Language: English
  • Description: Nationallizenz 142-005