5V5S

multi-drug efflux; membrane transport; RND superfamily; Drug resistance

Summary for 5V5S

• Entry DOI: 10.2210/pdb5v5s/pdb
• EMDB information: 8636
• Descriptor: Outer membrane protein TolC, Multidrug efflux pump subunit AcrA, Multidrug efflux pump subunit AcrB (3 entities in total)
• Functional Keywords: multi-drug efflux, membrane transport, rnd superfamily, drug resistance, membrane protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 12
• Total formula weight: 740586.44

Authors

wang, Z.,fan, G.,Hryc, C.F.,Blaza, J.N.,Serysheva, I.I.,Schmid, M.F.,Chiu, W.,Luisi, B.F.,Du, D. (deposition date: 2017-03-15, release date: 2017-04-19, Last modification date: 2024-11-20)

Primary citation

Wang, Z.,Fan, G.,Hryc, C.F.,Blaza, J.N.,Serysheva, I.I.,Schmid, M.F.,Chiu, W.,Luisi, B.F.,Du, D.
An allosteric transport mechanism for the AcrAB-TolC Multidrug Efflux Pump.
Elife, 6:-, 2017

PubMed 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 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.

PubMed: 28355133
DOI: 10.7554/eLife.24905

Experimental method

ELECTRON MICROSCOPY (6.5 Å)