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TitleFilaments from Ignicoccus hospitalis show diversity of packing in proteins containing N-terminal type IV pilin helices.
Journal, issue, pagesJ Mol Biol, Vol. 422, Issue 2, Page 274-281, Year 2012
Publish dateSep 14, 2012
AuthorsXiong Yu / Charles Goforth / Carolin Meyer / Reinhard Rachel / Reinhard Wirth / Gunnar F Schröder / Edward H Egelman /
PubMed AbstractBacterial motility is driven by the rotation of flagellar filaments that supercoil. The supercoiling involves the switching of coiled-coil protofilaments between two different states. In archaea, the ...Bacterial motility is driven by the rotation of flagellar filaments that supercoil. The supercoiling involves the switching of coiled-coil protofilaments between two different states. In archaea, the flagellar filaments responsible for motility are formed by proteins with distinct homology in their N-terminal portion to bacterial Type IV pilins. The bacterial pilins have a single N-terminal hydrophobic α-helix, not the coiled coil found in flagellin. We have used electron cryo-microscopy to study the adhesion filaments from the archaeon Ignicoccus hospitalis. While I. hospitalis is non-motile, these filaments make transitions between rigid stretches and curved regions and appear morphologically similar to true archaeal flagellar filaments. A resolution of ~7.5Å allows us to unambiguously build a model for the packing of these N-terminal α-helices, and this packing is different from several bacterial Type IV pili whose structure has been analyzed by electron microscopy and modeling. Our results show that the mechanism responsible for the supercoiling of bacterial flagellar filaments cannot apply to archaeal filaments.
External linksJ Mol Biol / PubMed:22659006 / PubMed Central
MethodsEM (helical sym.)
Resolution7.5 Å
Structure data

5423

3j1r

EMDB-5423, PDB-3j1r:
Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-terminal Type IV Pilin Helices
Method: EM (helical sym.) / Resolution: 7.5 Å

Source
  • ignicoccus hospitalis (archaea)
KeywordsCELL ADHESION / STRUCTURAL PROTEIN / helical polymer / flagellar filament

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