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Multiple entry pathways within the efflux transporter AcrB contribute to multidrug recognition
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Multiple entry pathways within the efflux transporter AcrB contribute to multidrug recognition
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Journal Article
Multiple entry pathways within the efflux transporter AcrB contribute to multidrug recognition
2018
Overview
AcrB is the major multidrug exporter in
Escherichia coli
. Although several substrate-entrances have been identified, the specificity of these various transport paths remains unclear. Here we present evidence for a substrate channel (channel 3) from the central cavity of the AcrB trimer, which is connected directly to the deep pocket without first passing the switch-loop and the proximal pocket . Planar aromatic cations, such as ethidium, prefer channel 3 to channels 1 and 2. The efflux through channel 3 increases by targeted mutations and is not in competition with the export of drugs such as minocycline and erythromycin through channels 1 and 2. A switch-loop mutant, in which the pathway from the proximal to the deep pocket is hindered, can export only channel 3-utilizing drugs. The usage of multiple entrances thus contributes to the recognition and transport of a wide range of drugs with different physicochemical properties.
Multidrug transporters possess several drug binding sites. Here the authors describe a transport path specific for planar aromatic cations in the
E. coli
multi-drug transporter AcrB.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 82/16
/ 82/29
/ 82/80
/ 82/81
/ Anti-Bacterial Agents - pharmacology
/ Cations
/ Channels
/ Drug Resistance, Multiple, Bacterial - genetics
/ Drugs
/ E coli
/ Efflux
/ Escherichia coli - drug effects
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - metabolism
/ Exports
/ Humanities and Social Sciences
/ Multidrug Resistance-Associated Proteins - chemistry
/ Multidrug Resistance-Associated Proteins - genetics
/ Multidrug Resistance-Associated Proteins - metabolism
/ Mutation
/ Proteins
/ Science
/ Signal Transduction - drug effects
