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TitleArchaeal flagellin combines a bacterial type IV pilin domain with an Ig-like domain.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 113, Issue 37, Page 10352-10357, Year 2016
Publish dateSep 13, 2016
AuthorsTatjana Braun / Matthijn R Vos / Nir Kalisman / Nicholas E Sherman / Reinhard Rachel / Reinhard Wirth / Gunnar F Schröder / Edward H Egelman /
PubMed AbstractThe bacterial flagellar apparatus, which involves ∼40 different proteins, has been a model system for understanding motility and chemotaxis. The bacterial flagellar filament, largely composed of a ...The bacterial flagellar apparatus, which involves ∼40 different proteins, has been a model system for understanding motility and chemotaxis. The bacterial flagellar filament, largely composed of a single protein, flagellin, has been a model for understanding protein assembly. This system has no homology to the eukaryotic flagellum, in which the filament alone, composed of a microtubule-based axoneme, contains more than 400 different proteins. The archaeal flagellar system is simpler still, in some cases having ∼13 different proteins with a single flagellar filament protein. The archaeal flagellar system has no homology to the bacterial one and must have arisen by convergent evolution. However, it has been understood that the N-terminal domain of the archaeal flagellin is a homolog of the N-terminal domain of bacterial type IV pilin, showing once again how proteins can be repurposed in evolution for different functions. Using cryo-EM, we have been able to generate a nearly complete atomic model for a flagellar-like filament of the archaeon Ignicoccus hospitalis from a reconstruction at ∼4-Å resolution. We can now show that the archaeal flagellar filament contains a β-sandwich, previously seen in the FlaF protein that forms the anchor for the archaeal flagellar filament. In contrast to the bacterial flagellar filament, where the outer globular domains make no contact with each other and are not necessary for either assembly or motility, the archaeal flagellin outer domains make extensive contacts with each other that largely determine the interesting mechanical properties of these filaments, allowing these filaments to flex.
External linksProc Natl Acad Sci U S A / PubMed:27578865 / PubMed Central
MethodsEM (helical sym.)
Resolution4.0 Å
Structure data

8298

5kyh

EMDB-8298, PDB-5kyh:
Structure of Iho670 Flagellar-like Filament
Method: EM (helical sym.) / Resolution: 4.0 Å

Source
  • ignicoccus hospitalis (archaea)
KeywordsCELL ADHESION / immunoglobulin fold / Type IV pili / flagellin

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