Wang, Zhao, Fan, Guizhen, Hryc, Corey F et al. (6 more authors) (2017) An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump. eLife. e24905. ISSN 2050-084X
Abstract
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.
Metadata
Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017, Wang et al. |
Keywords: | Allosteric Regulation, Anti-Bacterial Agents/metabolism, Carrier Proteins/chemistry, Cryoelectron Microscopy, Escherichia coli/chemistry, Escherichia coli Proteins/chemistry, Protein Conformation |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 21 Nov 2018 13:50 |
Last Modified: | 21 Dec 2023 00:15 |
Published Version: | https://doi.org/10.7554/eLife.24905 |
Status: | Published |
Refereed: | Yes |
Identification Number: | https://doi.org/10.7554/eLife.24905 |
Related URLs: |