3A69
Atomic model of the bacterial flagellar hook based on docking an X-ray derived structure and terminal two alpha-helices into an 7.1 angstrom resolution cryoEM map
Summary for 3A69
| Entry DOI | 10.2210/pdb3a69/pdb |
| EMDB information | 1647 |
| Descriptor | Flagellar hook protein flgE (1 entity in total) |
| Functional Keywords | the bacterial flagellar motor, universal joint, bacterial flagellum, motor protein |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium |
| Total number of polymer chains | 1 |
| Total formula weight | 42101.96 |
| Authors | |
| Primary citation | Fujii, T.,Kato, T.,Namba, K. Specific arrangement of alpha-helical coiled coils in the core domain of the bacterial flagellar hook for the universal joint function Structure, 17:1485-1493, 2009 Cited by PubMed Abstract: The bacterial flagellar hook is a short, highly curved tubular structure connecting the rotary motor to the filament acting as a helical propeller. The bending flexibility of the hook allows it to work as a universal joint. A partial atomic model of the hook revealed a sliding intersubunit domain interaction along the protofilament to produce bending flexibility. However, it remained unclear how the tightly packed inner core domains can still permit axial extension and compression. We report advances in cryoEM image analysis for high-resolution, high-throughput structural analysis and a density map of the hook that reveals most of the secondary structures, including the terminal alpha helices forming a coiled coil. The orientations and axial packing interactions of these two alpha helices are distinctly different from those of the filament, allowing them to have a room for axial compression and extension for bending flexibility without impairing the mechanical stability of the hook. PubMed: 19913483DOI: 10.1016/j.str.2009.08.017 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.1 Å) |
Structure validation
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