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-Structure paper
| Title | Architecture of the Bacterial Flagellar Distal Rod and Hook of . |
|---|---|
| Journal, issue, pages | Biomolecules, Vol. 9, Issue 7, Year 2019 |
| Publish date | Jul 7, 2019 |
 Authors | Yumiko Saijo-Hamano / Hideyuki Matsunami / Keiichi Namba / Katsumi Imada /  |
| PubMed Abstract | The bacterial flagellum is a large molecular complex composed of thousands of protein subunits for motility. The filamentous part of the flagellum, which is called the axial structure, consists of ...The bacterial flagellum is a large molecular complex composed of thousands of protein subunits for motility. The filamentous part of the flagellum, which is called the axial structure, consists of the filament, the hook, and the rods, with other minor components-the cap protein and the hook associated proteins. They share a common basic architecture of subunit arrangement, but each part shows quite distinct mechanical properties to achieve its specific function. The distal rod and the hook are helical assemblies of a single protein, FlgG and FlgE, respectively. They show a significant sequence similarity but have distinct mechanical characteristics. The rod is a rigid, straight cylinder, whereas the hook is a curved tube with high bending flexibility. Here, we report a structural model of the rod constructed by using the crystal structure of a core fragment of FlgG with a density map obtained previously by electron cryomicroscopy. Our structural model suggests that a segment called L-stretch plays a key role in achieving the distinct mechanical properties of the rod using a structurally similar component protein to that of the hook. |
 External links | Biomolecules / PubMed:31284631 / PubMed Central |
| Methods | X-ray diffraction / EM (helical sym.) |
| Resolution | 2 - 7.4 Å |
| Structure data |  PDB-6jf2:  PDB-6jzr:  PDB-6jzt: |
| Chemicals |  ChemComp-HOH: |
| Source |
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 Keywords |  STRUCTURAL PROTEIN / Bacterial flagellum / distal rod / MOTOR PROTEIN / rod protein / hook protein |
