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-Structure paper
Title | An allosteric transport mechanism for the AcrAB-TolC multidrug efflux pump. |
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Journal, issue, pages | Elife, Vol. 6, Year 2017 |
Publish date | Mar 29, 2017 |
Authors | Zhao Wang / Guizhen Fan / Corey F Hryc / James N Blaza / Irina I Serysheva / Michael F Schmid / Wah Chiu / Ben F Luisi / Dijun Du / |
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 ...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. |
External links | Elife / PubMed:28355133 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 3.2 - 6.5 Å |
Structure data | EMDB-3636, PDB-5ng5: EMDB-8636, PDB-5v5s: EMDB-8640: Asymmetric structure of AcrAB-TolC tripartite multi drug efflux pump PDB-5nc5: |
Chemicals | ChemComp-LMT: ChemComp-D12: ChemComp-D10: ChemComp-DD9: ChemComp-PUY: ChemComp-HEX: ChemComp-HOH: ChemComp-5QF: |
Source |
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Keywords | TRANSPORT PROTEIN / Membrane transporter / Multidrug efflux pump / MEMBRANE PROTEIN / multi-drug efflux; membrane transport; RND superfamily; Drug resistance / multi-drug efflux / membrane transport / RND superfamily / Drug resistance |