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An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump
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An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump
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An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump
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Journal Article
An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump
2017
Overview
Bacterial efflux pumps confer multidrug resistance by transporting diverse antibiotics from the cell. In Gram-negative bacteria, some of these pumps form multi-protein assemblies that span the cell envelope. Here, we report the near-atomic resolution cryoEM structures of the Escherichia coli AcrAB-TolC multidrug efflux pump in resting and drug transport states, revealing a quaternary structural switch that allosterically couples and synchronizes initial ligand binding with channel opening. Within the transport-activated state, the channel remains open even though the pump cycles through three distinct conformations. Collectively, our data provide a dynamic mechanism for the assembly and operation of the AcrAB-TolC pump.
Publisher
eLife Science Publications, Ltd,eLife Sciences Publications Ltd,eLife Sciences Publications, Ltd
Subject
/ AcrZ
/ Analysis
/ Anti-Bacterial Agents - metabolism
/ Biophysics and Structural Biology
/ Carb
/ Carrier Proteins - chemistry
/ Carrier Proteins - metabolism
/ Escherichia coli - chemistry
/ Escherichia coli - enzymology
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - metabolism
/ Ligands
/ Protein-protein interactions
/ Proteins
/ TolC
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