Functional relevance of AcrB Trimerization in pump assembly and substrate binding.
AcrB is a multidrug transporter in the inner membrane of Escherichia coli. It is an obligate homotrimer and forms a tripartite efflux complex with AcrA and TolC. AcrB is the engine of the efflux machinery and determines substrate specificity. Active efflux depends on several functional features incl...
Main Authors: | Wei Lu, Meng Zhong, Qian Chai, Zhaoshuai Wang, Linliang Yu, Yinan Wei |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2014-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3925222?pdf=render |
Similar Items
-
Repressive mutations restore function-loss caused by the disruption of trimerization in Escherichia coli multidrug transporter AcrB
by: Zhaoshuai eWang, et al.
Published: (2015-01-01) -
Probing the Dynamics of AcrB Through Disulfide Bond Formation
by: Prasangi Rajapaksha, et al.
Published: (2020-08-01) -
Substrate binding accelerates the conformational transitions and substrate dissociation in multidrug efflux transporter AcrB
by: Beibei eWang, et al.
Published: (2015-04-01) -
Structures of Gate Loop Variants of the AcrB Drug Efflux Pump Bound by Erythromycin Substrate.
by: Abdessamad Ababou, et al.
Published: (2016-01-01) -
Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB
by: Thomas Eicher, et al.
Published: (2014-09-01)