9N8H
In situ sheathed flagellar filament of Vibrio cholerae resolved with helical reconstruction.
Summary for 9N8H
| Entry DOI | 10.2210/pdb9n8h/pdb |
| EMDB information | 49129 |
| Descriptor | Flagellin D (1 entity in total) |
| Functional Keywords | in situ cryo-em, sheathed flagellar filament, flad vibrio cholerae., motor protein |
| Biological source | Vibrio cholerae O1 biovar El Tor str. N16961 |
| Total number of polymer chains | 33 |
| Total formula weight | 1318020.26 |
| Authors | Wangbiao, G.,Jun, L. (deposition date: 2025-02-08, release date: 2025-09-24, Last modification date: 2025-11-12) |
| Primary citation | Guo, W.,Zhang, S.,Park, J.H.,Stanton, V.,Asp, M.,Herrera, H.,Tai, J.B.,Yue, J.,Wang, J.,Guo, J.,Kumar, R.,Botting, J.M.,Wu, S.,Yan, J.,Klose, K.E.,Yildiz, F.H.,Liu, J. Structures of the sheathed flagellum reveal mechanisms of assembly and rotation in Vibrio cholerae. Nat Microbiol, 2025 Cited by PubMed Abstract: Motility promotes the complex life cycle and infectious capabilities of Vibrio cholerae and is driven by rotation of a single polar flagellum. The flagellar filament comprises four flagellin proteins (FlaA-D) and is covered by a membranous sheath continuous with the outer membrane. Here we combine in situ cryo-electron microscopy single-particle analysis, fluorescence microscopy and molecular genetics to determine 2.92-3.43 Å structures of the sheathed flagellar filament from intact bacteria. Our data reveal the spatial arrangement of FlaA-D, showing that FlaA localizes at the cell pole and functions as a template for filament assembly involving multiple flagellins. Unlike unsheathed flagellar filaments, the sheathed filament from V. cholerae possesses a highly conserved core but a smooth, hydrophilic surface adjacent to the membranous sheath. A tiny conformational change at the single flagellin level results in a supercoiled filament and curved membranous sheath, supporting a model wherein the filament rotates separately from the sheath, enabling the distinct motility of V. cholerae. PubMed: 41174224DOI: 10.1038/s41564-025-02161-x PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.73 Å) |
Structure validation
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