9EN1
FliG interacting domain of SpFlhF (FID)
Summary for 9EN1
| Entry DOI | 10.2210/pdb9en1/pdb |
| Descriptor | Flagellar biosynthesis protein FlhF (1 entity in total) |
| Functional Keywords | flagellation, flagellar assembly, gtpase, signaling protein |
| Biological source | Shewanella putrefaciens CN-32 |
| Total number of polymer chains | 12 |
| Total formula weight | 70474.70 |
| Authors | Dornes, A.,Mais, C.-N.,Bange, G. (deposition date: 2024-03-12, release date: 2025-03-26, Last modification date: 2026-10-14) |
| Primary citation | Dornes, A.,Schmidt, L.M.,Mais, C.N.,Hook, J.C.,Pane-Farre, J.,Kressler, D.,Thormann, K.,Bange, G. Polar confinement of a macromolecular machine by an SRP-type GTPase. Nat Commun, 15:5797-5797, 2024 Cited by PubMed Abstract: The basal structure of the bacterial flagellum includes a membrane embedded MS-ring (formed by multiple copies of FliF) and a cytoplasmic C-ring (composed of proteins FliG, FliM and FliN). The SRP-type GTPase FlhF is required for directing the initial flagellar protein FliF to the cell pole, but the mechanisms are unclear. Here, we show that FlhF anchors developing flagellar structures to the polar landmark protein HubP/FimV, thereby restricting their formation to the cell pole. Specifically, the GTPase domain of FlhF interacts with HubP, while a structured domain at the N-terminus of FlhF binds to FliG. FlhF-bound FliG subsequently engages with the MS-ring protein FliF. Thus, the interaction of FlhF with HubP and FliG recruits a FliF-FliG complex to the cell pole. In addition, the modulation of FlhF activity by the MinD-type ATPase FlhG controls the interaction of FliG with FliM-FliN, thereby regulating the progression of flagellar assembly at the pole. PubMed: 38987236DOI: 10.1038/s41467-024-50274-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.01 Å) |
Structure validation
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