3A5X
L-type straight flagellar filament made of full-length flagellin
Summary for 3A5X
| Entry DOI | 10.2210/pdb3a5x/pdb |
| EMDB information | 1641 |
| Descriptor | Flagellin (1 entity in total) |
| Functional Keywords | flagellin, flagellar filament, helical reconstruction, bacterial flagellum, secreted, structural protein, motor protein |
| Biological source | Salmonella typhimurium |
| Total number of polymer chains | 1 |
| Total formula weight | 51537.18 |
| Authors | Maki-Yonekura, S.,Yonekura, K.,Namba, K. (deposition date: 2009-08-13, release date: 2010-03-16, Last modification date: 2024-03-13) |
| Primary citation | Maki-Yonekura, S.,Yonekura, K.,Namba, K. Conformational change of flagellin for polymorphic supercoiling of the flagellar filament Nat.Struct.Mol.Biol., 17:417-422, 2010 Cited by PubMed Abstract: The bacterial flagellar filament is a helical propeller rotated by the flagellar motor for bacterial locomotion. The filament is a supercoiled assembly of a single protein, flagellin, and is formed by 11 protofilaments. For bacterial taxis, the reversal of motor rotation switches the supercoil between left- and right-handed, both of which arise from combinations of two distinct conformations and packing interactions of the L-type and R-type protofilaments. Here we report an atomic model of the L-type straight filament by electron cryomicroscopy and helical image analysis. Comparison with the R-type structure shows interesting features: an orientation change of the outer core domains (D1) against the inner core domains (D0) showing almost invariant orientation and packing, a conformational switching within domain D1, and the conformational flexibility of domains D0 and D1 with their spoke-like connection for tight molecular packing. PubMed: 20228803DOI: 10.1038/nsmb.1774 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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