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

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.

SUBMITTER: Wang Z 

PROVIDER: S-EPMC5404916 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature