5ng5
From Proteopedia
multi-drug efflux; membrane transport; RND superfamily; Drug resistance
Structural highlights
FunctionACRA_ECOLI AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm.[1] Publication Abstract from PubMedBacterial 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. An allosteric transport mechanism for the AcrAB-TolC Multidrug Efflux Pump.,Wang Z, Fan G, Hryc CF, Blaza JN, Serysheva II, Schmid MF, Chiu W, Luisi BF, Du D Elife. 2017 Mar 29;6. pii: e24905. doi: 10.7554/eLife.24905. PMID:28355133[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Escherichia coli | Large Structures | Blaza JN | Chiu W | Du D | Fan G | Hryc CF | Luisi BF | Schmid MF | Serysheva II | Wang Z
