8ZDU
Structure of the RBM3 ring of Salmonella flagellar MS-ring protein FliF with C34 symmetry applied
Summary for 8ZDU
| Entry DOI | 10.2210/pdb8zdu/pdb |
| EMDB information | 60009 |
| Descriptor | Flagellar M-ring protein (1 entity in total) |
| Functional Keywords | bacterial flagellum, flagellar assembly, electron cryomicroscopy, ms-ring, type iii secretion system, salmonella, motor protein |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium |
| Total number of polymer chains | 34 |
| Total formula weight | 2084051.93 |
| Authors | Kinoshita, M.,Makino, F.,Miyata, T.,Imada, K.,Minamino, T.,Namba, K. (deposition date: 2024-05-03, release date: 2025-01-01, Last modification date: 2025-04-23) |
| Primary citation | Kinoshita, M.,Makino, F.,Miyata, T.,Imada, K.,Namba, K.,Minamino, T. Structural basis for assembly and function of the Salmonella flagellar MS-ring with three different symmetries. Commun Biol, 8:61-61, 2025 Cited by PubMed Abstract: The flagellar MS-ring is the initial template for flagellar assembly and houses the flagellar protein export complex. The MS-ring has three parts of different symmetries within the ring structure by assembly of FliF subunits in two different conformations with distinct arrangements of three ring-building motifs, RBM1, RBM2, and RBM3. However, it remains unknown how these symmetries are generated. A combination of cryoEM structure and structure-based mutational analyses demonstrates that the well-conserved DQxGxxL motif in the RBM2-RBM3 hinge loop allows RBM2 to take two different orientations relative to RBM3. Of 34 FliF subunits of the MS-ring in the basal body, 23 RBM2 domains form an inner ring with a central pore that accommodates the flagellar protein export complex, and the remaining 11 RBM2 domains form 11 cog-like structures together with RBM1 domains just outside the inner RBM2-ring. We propose that a dimer of FliF with two different conformations initiates MS-ring assembly. PubMed: 39820129DOI: 10.1038/s42003-025-07485-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.5 Å) |
Structure validation
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