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Cited by 275

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump

Open access
Wang, Zhao, Fan, Guizhen, Hryc, Corey F, Blaza, James N, Serysheva, Irina I, Schmid, Michael F, Chiu, Wah, Luisi, Ben F, Du, Dijun·2017·eLife

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.

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Crossref · 10.7554/elife.24905

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Metadata

Authors
Wang, Z., Fan, G., Hryc, C. F., Blaza, J. N., Serysheva, I. I., Schmid, M. F., Chiu, W., Luisi, B. F., & Du, D.
Venue
eLife
Published
2017-03-29
Volume
6
ISSN
2050-084X (ISSN-L)
OpenAlex
W2597700712
Cited by
275
References
3
FWCI
9.52
Type
journal article
Language
en
Open access
gold

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CoChat. (2026). Citation check: An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump. https://app.cochat.ai/papers/10.7554/elife.24905
The paper
Wang, Z., Fan, G., Hryc, C. F., Blaza, J. N., Serysheva, I. I., Schmid, M. F., Chiu, W., Luisi, B. F., & Du, D. (2017). An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump. eLife. https://doi.org/10.7554/elife.24905

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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