5NG5

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

Summary for 5NG5

• Entry DOI: 10.2210/pdb5ng5/pdb
• EMDB information: 3636
• Descriptor: Multidrug efflux pump subunit AcrA, Outer membrane protein TolC, Multidrug efflux pump subunit AcrB, ... (5 entities in total)
• Functional Keywords: multi-drug efflux; membrane transport; rnd superfamily; drug resistance, membrane protein
• Biological source: Escherichia coli; More
• Cellular location: Cell inner membrane ; Lipid- anchor : P0AE06; Cell outer membrane ; Multi-pass membrane protein : P02930; Cell inner membrane ; Multi- pass membrane protein : P31224; Cell inner membrane ; Single-pass membrane protein : P0AAW9
• Total number of polymer chains: 15
• Total formula weight: 760715.11

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: 2017-03-16, release date: 2017-04-19, Last modification date: 2017-08-02)

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)