Summary for 8T8P
| Entry DOI | 10.2210/pdb8t8p/pdb |
| EMDB information | 41100 41101 41102 41103 41104 |
| Descriptor | Flagellar M-ring protein (1 entity in total) |
| Functional Keywords | ms-ring, symmetry mismatch, flagellar component, membrane protein, motor protein |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium |
| Total number of polymer chains | 33 |
| Total formula weight | 2022756.28 |
| Authors | Singh, P.K.,Iverson, T.M. (deposition date: 2023-06-23, release date: 2024-02-28, Last modification date: 2024-08-21) |
| Primary citation | Singh, P.K.,Sharma, P.,Afanzar, O.,Goldfarb, M.H.,Maklashina, E.,Eisenbach, M.,Cecchini, G.,Iverson, T.M. CryoEM structures reveal how the bacterial flagellum rotates and switches direction. Nat Microbiol, 9:1271-1281, 2024 Cited by PubMed Abstract: Bacterial chemotaxis requires bidirectional flagellar rotation at different rates. Rotation is driven by a flagellar motor, which is a supercomplex containing multiple rings. Architectural uncertainty regarding the cytoplasmic C-ring, or 'switch', limits our understanding of how the motor transmits torque and direction to the flagellar rod. Here we report cryogenic electron microscopy structures for Salmonella enterica serovar typhimurium inner membrane MS-ring and C-ring in a counterclockwise pose (4.0 Å) and isolated C-ring in a clockwise pose alone (4.6 Å) and bound to a regulator (5.9 Å). Conformational differences between rotational poses include a 180° shift in FliF/FliG domains that rotates the outward-facing MotA/B binding site to inward facing. The regulator has specificity for the clockwise pose by bridging elements unique to this conformation. We used these structures to propose how the switch reverses rotation and transmits torque to the flagellum, which advances the understanding of bacterial chemotaxis and bidirectional motor rotation. PubMed: 38632342DOI: 10.1038/s41564-024-01674-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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