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Instruments / Technical Area	Publication Details	Published	Actions
I24-Microfocus Macromolecular Crystallography Krios I-Titan Krios I at Diamond	An allosteric transport mechanism for the AcrAB-TolC Multidrug Efflux Pump Zhao Wang , Guizhen Fan , Corey F Hryc , James N. Blaza , Irina I. Serysheva , Michael F Schmid , Wah Chiu , Ben Luisi , Dijun Du Elife 6 DOI: 10.7554/eLife.24905 Diamond Proposal Number(s): [14043] Open Access Show Abstract ▼ 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.	Mar 2017

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