1UCU
R-type straight flagellar filament made of full-length flagellin
Summary for 1UCU
| Entry DOI | 10.2210/pdb1ucu/pdb |
| Descriptor | phase 1 Flagellin (1 entity in total) |
| Functional Keywords | flagellin, flagellar filament, helical reconstruction, structural protein |
| Biological source | Salmonella typhimurium |
| Cellular location | Secreted: P06179 |
| Total number of polymer chains | 1 |
| Total formula weight | 51551.20 |
| Authors | Yonekura, K.,Maki-Yonekura, S.,Namba, K. (deposition date: 2003-04-22, release date: 2003-08-12, Last modification date: 2024-03-13) |
| Primary citation | Yonekura, K.,Maki-Yonekura, S.,Namba, K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy NATURE, 424:643-650, 2003 Cited by PubMed Abstract: The bacterial flagellar filament is a helical propeller for bacterial locomotion. It is a helical assembly of a single protein, flagellin, and its tubular structure is formed by 11 protofilaments in two distinct conformations, L- and R-type, for supercoiling. The X-ray crystal structure of a flagellin fragment lacking about 100 terminal residues revealed the protofilament structure, but the full filament structure is still essential for understanding the mechanism of supercoiling and polymerization. Here we report a complete atomic model of the R-type filament by electron cryomicroscopy. A density map obtained from image data up to 4 A resolution shows the feature of alpha-helical backbone and some large side chains. The atomic model built on the map reveals intricate molecular packing and an alpha-helical coiled coil formed by the terminal chains in the inner core of the filament, with its intersubunit hydrophobic interactions having an important role in stabilizing the filament. PubMed: 12904785DOI: 10.1038/nature01830 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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