7D84
34-fold symmetry Salmonella S ring formed by full-length FliF
Summary for 7D84
| Entry DOI | 10.2210/pdb7d84/pdb |
| EMDB information | 30612 |
| Descriptor | Flagellar M-ring protein (1 entity in total) |
| Functional Keywords | flagellar motor, type iii protein export system, transmembrane protein complex, torque generation, membrane protein |
| Biological source | Salmonella enterica serovar Typhimurium |
| Total number of polymer chains | 34 |
| Total formula weight | 2084051.93 |
| Authors | Kawamoto, A.,Miyata, T.,Makino, F.,Kinoshita, M.,Minamino, T.,Imada, K.,Kato, T.,Namba, K. (deposition date: 2020-10-07, release date: 2021-05-19, Last modification date: 2024-03-27) |
| Primary citation | Kawamoto, A.,Miyata, T.,Makino, F.,Kinoshita, M.,Minamino, T.,Imada, K.,Kato, T.,Namba, K. Native flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries. Nat Commun, 12:4223-4223, 2021 Cited by PubMed Abstract: The bacterial flagellar MS ring is a transmembrane complex acting as the core of the flagellar motor and template for flagellar assembly. The C ring attached to the MS ring is involved in torque generation and rotation switch, and a large symmetry mismatch between these two rings has been a long puzzle, especially with respect to their role in motor function. Here, using cryoEM structural analysis of the flagellar basal body and the MS ring formed by full-length FliF from Salmonella enterica, we show that the native MS ring is formed by 34 FliF subunits with no symmetry variation. Symmetry analysis of the C ring shows a variation with a peak at 34-fold, suggesting flexibility in C ring assembly. Finally, our data also indicate that FliF subunits assume two different conformations, contributing differentially to the inner and middle parts of the M ring and thus resulting in 23- and 11-fold subsymmetries in the inner and middle M ring, respectively. The internal core of the M ring, formed by 23 subunits, forms a hole of the right size to accommodate the protein export gate. PubMed: 34244518DOI: 10.1038/s41467-021-24507-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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