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TitleComplete structure of the bacterial flagellar hook reveals extensive set of stabilizing interactions.
Journal, issue, pagesNat Commun, Vol. 7, Page 13425, Year 2016
Publish dateNov 4, 2016
AuthorsHideyuki Matsunami / Clive S Barker / Young-Ho Yoon / Matthias Wolf / Fadel A Samatey /
PubMed AbstractThe bacterial flagellar hook is a tubular helical structure made by the polymerization of multiple copies of a protein, FlgE. Here we report the structure of the hook from Campylobacter jejuni by ...The bacterial flagellar hook is a tubular helical structure made by the polymerization of multiple copies of a protein, FlgE. Here we report the structure of the hook from Campylobacter jejuni by cryo-electron microscopy at a resolution of 3.5 Å. On the basis of this structure, we show that the hook is stabilized by intricate inter-molecular interactions between FlgE molecules. Extra domains in FlgE, found only in Campylobacter and in related bacteria, bring more stability and robustness to the hook. Functional experiments suggest that Campylobacter requires an unusually strong hook to swim without its flagella being torn off. This structure reveals details of the quaternary organization of the hook that consists of 11 protofilaments. Previous study of the flagellar filament of Campylobacter by electron microscopy showed its quaternary structure made of seven protofilaments. Therefore, this study puts in evidence the difference between the quaternary structures of a bacterial filament and its hook.
External linksNat Commun / PubMed:27811912 / PubMed Central
MethodsEM (helical sym.)
Resolution3.5 Å
Structure data

8179

5jxl

EMDB-8179: Campylobacter Hook
PDB-5jxl: Cryo-EM structure of the flagellar hook of Campylobacter jejuni
Method: EM (helical sym.) / Resolution: 3.5 Å

Source
  • campylobacter jejuni subsp. jejuni 81116 (Campylobacter)
KeywordsMOTOR PROTEIN / Campylobacter jejuni / helical assembly of FlgE / flagellar hook

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