6T17
Cryo-EM structure of the wild-type flagellar filament of the Firmicute Kurthia
This is a non-PDB format compatible entry.
Summary for 6T17
| Entry DOI | 10.2210/pdb6t17/pdb |
| EMDB information | 10362 |
| Descriptor | Flagellin (1 entity in total) |
| Functional Keywords | gram-positive bacteria flagella, helical, wild-type, protein fibril |
| Biological source | Kurthia sp. 11kri321 |
| Total number of polymer chains | 44 |
| Total formula weight | 1299322.42 |
| Authors | Blum, T.B.,Abrahams, J.P. (deposition date: 2019-10-03, release date: 2019-10-30, Last modification date: 2024-05-22) |
| Primary citation | Blum, T.B.,Filippidou, S.,Fatton, M.,Junier, P.,Abrahams, J.P. The wild-type flagellar filament of the Firmicute Kurthia at 2.8 angstrom resolution in vivo. Sci Rep, 9:14948-14948, 2019 Cited by PubMed Abstract: Bacteria swim and swarm by rotating the micrometers long, helical filaments of their flagella. They change direction by reversing their flagellar rotation, which switches the handedness of the filament's supercoil. So far, all studied functional filaments are composed of a mixture of L- and R-state flagellin monomers. Here we show in a study of the wild type Firmicute Kurthia sp., that curved, functional filaments can adopt a conformation in vivo that is closely related to a uniform, all-L-state. This sheds additional light on transitions of the flagellar supercoil and uniquely reveals the atomic structure of a wild-type flagellar filament in vivo, including six residues showing clearly densities of O-linked glycosylation. PubMed: 31628388DOI: 10.1038/s41598-019-51440-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.8 Å) |
Structure validation
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