6IOL
Cryo-EM structure of multidrug efflux pump MexAB-OprM (60 degree state)
Summary for 6IOL
| Entry DOI | 10.2210/pdb6iol/pdb |
| EMDB information | 9696 |
| Descriptor | Multidrug resistance protein MexA, Outer membrane protein OprM, Multidrug resistance protein MexB (3 entities in total) |
| Functional Keywords | multidrug resistance, efflux, complex, membrane protein |
| Biological source | Pseudomonas aeruginosa More |
| Total number of polymer chains | 12 |
| Total formula weight | 729795.80 |
| Authors | Tsutsumi, K.,Yonehara, R.,Nakagawa, A.,Yamashita, E. (deposition date: 2018-10-30, release date: 2019-04-03, Last modification date: 2024-03-27) |
| Primary citation | Tsutsumi, K.,Yonehara, R.,Ishizaka-Ikeda, E.,Miyazaki, N.,Maeda, S.,Iwasaki, K.,Nakagawa, A.,Yamashita, E. Structures of the wild-type MexAB-OprM tripartite pump reveal its complex formation and drug efflux mechanism. Nat Commun, 10:1520-1520, 2019 Cited by PubMed Abstract: In Pseudomonas aeruginosa, MexAB-OprM plays a central role in multidrug resistance by ejecting various drug compounds, which is one of the causes of serious nosocomial infections. Although the structures of the components of MexAB-OprM have been solved individually by X-ray crystallography, no structural information for fully assembled pumps from P. aeruginosa were previously available. In this study, we present the structure of wild-type MexAB-OprM in the presence or absence of drugs at near-atomic resolution. The structure reveals that OprM does not interact with MexB directly, and that it opens its periplasmic gate by forming a complex. Furthermore, we confirm the residues essential for complex formation and observed a movement of the drug entrance gate. Based on these results, we propose mechanisms for complex formation and drug efflux. PubMed: 30944318DOI: 10.1038/s41467-019-09463-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.76 Å) |
Structure validation
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