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TitleStructure of the bacterial flagellar hook and implication for the molecular universal joint mechanism.
Journal, issue, pagesNature, Vol. 431, Issue 7012, Page 1062-1068, Year 2004
Publish dateOct 28, 2004
AuthorsFadel A Samatey / Hideyuki Matsunami / Katsumi Imada / Shigehiro Nagashima / Tanvir R Shaikh / Dennis R Thomas / James Z Chen / David J Derosier / Akio Kitao / Keiichi Namba /
PubMed AbstractThe bacterial flagellum is a motile organelle, and the flagellar hook is a short, highly curved tubular structure that connects the flagellar motor to the long filament acting as a helical propeller. ...The bacterial flagellum is a motile organelle, and the flagellar hook is a short, highly curved tubular structure that connects the flagellar motor to the long filament acting as a helical propeller. The hook is made of about 120 copies of a single protein, FlgE, and its function as a nano-sized universal joint is essential for dynamic and efficient bacterial motility and taxis. It transmits the motor torque to the helical propeller over a wide range of its orientation for swimming and tumbling. Here we report a partial atomic model of the hook obtained by X-ray crystallography of FlgE31, a major proteolytic fragment of FlgE lacking unfolded terminal regions, and by electron cryomicroscopy and three-dimensional helical image reconstruction of the hook. The model reveals the intricate molecular interactions and a plausible switching mechanism for the hook to be flexible in bending but rigid against twisting for its universal joint function.
External linksNature / PubMed:15510139
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-1wlg:
Crystal structure of FlgE31, a major fragment of the hook protein
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • salmonella typhimurium (bacteria)
KeywordsSTRUCTURAL PROTEIN / EAR-& motif

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