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Structural and functional aspects of the multidrug efflux pump AcrB
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Thomas Eicher
Published/Copyright:
May 20, 2009
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
Received: 2009-3-1
Accepted: 2009-4-29
Published Online: 2009-05-20
Published in Print: 2009-08-01
©2009 by Walter de Gruyter Berlin New York
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Keywords for this article
AcrB;
alternate access transport mechanism;
antibiotic resistance;
binding change mechanism;
drug transport;
membrane protein structure;
multiple drug efflux pump
Articles in the same Issue
- Guest Editorial
- Highlight: The gatekeepers of life yield their secrets
- Highlight: Membrane Transport and Communication
- First structural insights into the TpsB/Omp85 superfamily
- Regulative interactions of the osmosensing C-terminal domain in the trimeric glycine betaine transporter BetP from Corynebacteriumglutamicum
- Structural and functional aspects of the multidrug efflux pump AcrB
- From the Sec complex to the membrane insertase YidC
- Emerging roles of mitochondrial membrane dynamics in health and disease
- Mitochondrial tRNA import – the challenge to understand has just begun
- Multiple pathways for mitochondrial protein traffic
- Challenges to our current view on chloroplasts
- Molecular interactions within the plant TOC complex
- Protein transport across the peroxisomal membrane
- On the fate of early endosomes
- ZMPSTE24, an integral membrane zinc metalloprotease with a connection to progeroid disorders
- Protein targeting by the signal recognition particle
- The peptide-loading complex – antigen translocation and MHC class I loading
- Protein-lipid interactions: paparazzi hunting for snap-shots
- The nanodisc: a novel tool for membrane protein studies
- NMR and EPR studies of membrane transporters
