3J1R

Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-terminal Type IV Pilin Helices

3J1R の概要

• エントリーDOI: 10.2210/pdb3j1r/pdb
• EMDBエントリー: 5423
• 分子名称: archaeal adhesion filament core (1 entity in total)
• 機能のキーワード: helical polymer, flagellar filament, cell adhesion, structural protein
• 由来する生物種: Ignicoccus hospitalis
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 56917.14

構造登録者

Yu, X.,Goforth, C.,Meyer, C.,Rachel, R.,Wirth, R.,Schroeder, G.F.,Egelman, E.H. (登録日: 2012-05-18, 公開日: 2012-06-20, 最終更新日: 2024-02-21)

主引用文献

Yu, X.,Goforth, C.,Meyer, C.,Rachel, R.,Wirth, R.,Schroder, G.F.,Egelman, E.H.
Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-Terminal Type IV Pilin Helices.
J.Mol.Biol., 422:274-281, 2012

PubMed Abstract: 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.

PubMed: 22659006
DOI: 10.1016/j.jmb.2012.05.031

実験手法

ELECTRON MICROSCOPY (7.5 Å)