5nc5
Crystal structure of AcrBZ in complex with antibiotic puromycinCrystal structure of AcrBZ in complex with antibiotic puromycin
Structural highlights
Function[ACRB_ECOLI] AcrAB is a drug efflux protein with a broad substrate specificity.[1] [2] [3] [ACRZ_ECO57] AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with a broad substrate specificity. This protein binds to AcrB and is required for efflux of some but not all substrates, suggesting it may influence the specificity of drug export.[HAMAP-Rule:MF_01484] 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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