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TitleIdentical folds used for distinct mechanical functions of the bacterial flagellar rod and hook.
Journal, issue, pagesNat Commun, Vol. 8, Page 14276, Year 2017
Publish dateJan 25, 2017
AuthorsTakashi Fujii / Takayuki Kato / Koichi D Hiraoka / Tomoko Miyata / Tohru Minamino / Fabienne F V Chevance / Kelly T Hughes / Keiichi Namba /
PubMed AbstractThe bacterial flagellum is a motile organelle driven by a rotary motor, and its axial portions function as a drive shaft (rod), a universal joint (hook) and a helical propeller (filament). The rod ...The bacterial flagellum is a motile organelle driven by a rotary motor, and its axial portions function as a drive shaft (rod), a universal joint (hook) and a helical propeller (filament). The rod and hook are directly connected to each other, with their subunit proteins FlgG and FlgE having 39% sequence identity, but show distinct mechanical properties; the rod is straight and rigid as a drive shaft whereas the hook is flexible in bending as a universal joint. Here we report the structure of the rod and comparison with that of the hook. While these two structures have the same helical symmetry and repeat distance and nearly identical folds of corresponding domains, the domain orientations differ by ∼7°, resulting in tight and loose axial subunit packing in the rod and hook, respectively, conferring the rigidity on the rod and flexibility on the hook. This provides a good example of versatile use of a protein structure in biological organisms.
External linksNat Commun / PubMed:28120828 / PubMed Central
MethodsEM (helical sym.)
Resolution7.4 Å
Structure data

6683

5wrh

EMDB-6683: The 7 angstrom resolution CryoEM map of the bacterial flagellar polyrod
PDB-5wrh: FlgG structure based on the CryoEM map of the bacterial flagellar polyrod
Method: EM (helical sym.) / Resolution: 7.4 Å

Source
  • salmonella typhimurium (strain lt2 / sgsc1412 / atcc 700720) (bacteria)
KeywordsMOTOR PROTEIN / the bacterial flagellar motor

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