5NC5

Crystal structure of AcrBZ in complex with antibiotic puromycin

Summary for 5NC5

• Entry DOI: 10.2210/pdb5nc5/pdb
• Descriptor: Multidrug efflux pump subunit AcrB, DARPin, Multidrug efflux pump accessory protein AcrZ, ... (10 entities in total)
• Functional Keywords: membrane transporter, multidrug efflux pump, transport protein
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 8
• Total formula weight: 402491.05

Authors

Du, D.,Luisi, B. (deposition date: 2017-03-03, release date: 2017-04-12, Last modification date: 2024-01-17)

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

X-RAY DIFFRACTION (3.2 Å)