Summary for 5O66
| Entry DOI | 10.2210/pdb5o66/pdb |
| EMDB information | 8640 |
| Descriptor | Outer membrane protein TolC, Multidrug efflux pump subunit AcrA, Multidrug efflux pump subunit AcrB, ... (4 entities in total) |
| Functional Keywords | multidrug efflux pump, membrane transporter, membrane protein |
| Biological source | Escherichia coli K12 More |
| Total number of polymer chains | 15 |
| Total formula weight | 759135.04 |
| Authors | Du, D.,Luisi, B.F. (deposition date: 2017-06-05, release date: 2017-06-14, Last modification date: 2025-07-02) |
| 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 Cited by 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: 28355133DOI: 10.7554/eLife.24905 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.9 Å) |
Structure validation
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