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TitleIn situ structure of the AcrAB-TolC efflux pump at subnanometer resolution.
Journal, issue, pagesStructure, Vol. 30, Issue 1, Page 107-113.e3, Year 2022
Publish dateJan 6, 2022
AuthorsMuyuan Chen / Xiaodong Shi / Zhili Yu / Guizhen Fan / Irina I Serysheva / Matthew L Baker / Ben F Luisi / Steven J Ludtke / Zhao Wang /
PubMed AbstractThe tripartite AcrAB-TolC assembly, which spans both the inner and outer membranes in Gram-negative bacteria, is an efflux pump that contributes to multidrug resistance. Here, we present the in situ ...The tripartite AcrAB-TolC assembly, which spans both the inner and outer membranes in Gram-negative bacteria, is an efflux pump that contributes to multidrug resistance. Here, we present the in situ structure of full-length Escherichia coli AcrAB-TolC determined at 7 Å resolution by electron cryo-tomography. The TolC channel penetrates the outer membrane bilayer through to the outer leaflet and exhibits two different configurations that differ by a 60° rotation relative to the AcrB position in the pump assembly. AcrA protomers interact directly with the inner membrane and with AcrB via an interface located in proximity to the AcrB ligand-binding pocket. Our structural analysis suggests that these AcrA-bridged interactions underlie an allosteric mechanism for transmitting drug-evoked signals from AcrB to the TolC channel within the pump. Our study demonstrates the power of in situ electron cryo-tomography, which permits critical insights into the function of bacterial efflux pumps.
External linksStructure / PubMed:34506732 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution7.0 Å
Structure data

EMDB-24609: Subnanometer in situ structure of the AcrAB-TolC efflux pump bound with MBX
Method: EM (subtomogram averaging) / Resolution: 7.0 Å

Source
  • Escherichia coli (E. coli)

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