1WLG

Crystal structure of FlgE31, a major fragment of the hook protein

1WLG の概要

• エントリーDOI: 10.2210/pdb1wlg/pdb
• 関連するPDBエントリー: 1IO1 1UCU
• 分子名称: Flagellar hook protein flgE (2 entities in total)
• 機能のキーワード: ear-& motif, structural protein
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Bacterial flagellum basal body (By similarity): P0A1J1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62670.17

構造登録者

Samatey, F.A.,Matsunami, H.,Imada, K.,Nagashima, S.,Shaikh, T.R.,Thomas, D.R.,DeRosier, D.J.,Kitao, A.,Namba, K. (登録日: 2004-06-25, 公開日: 2004-11-02, 最終更新日: 2024-03-13)

主引用文献

Samatey, F.A.,Matsunami, H.,Imada, K.,Nagashima, S.,Shaikh, T.R.,Thomas, D.R.,Chen, J.Z.,Derosier, D.J.,Kitao, A.,Namba, K.
Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism.
Nature, 431:1062-1068, 2004

PubMed Abstract: The bacterial flagellum is a motile organelle, and the flagellar hook is a short, highly curved tubular structure that connects the flagellar motor to the long filament acting as a helical propeller. The hook is made of about 120 copies of a single protein, FlgE, and its function as a nano-sized universal joint is essential for dynamic and efficient bacterial motility and taxis. It transmits the motor torque to the helical propeller over a wide range of its orientation for swimming and tumbling. Here we report a partial atomic model of the hook obtained by X-ray crystallography of FlgE31, a major proteolytic fragment of FlgE lacking unfolded terminal regions, and by electron cryomicroscopy and three-dimensional helical image reconstruction of the hook. The model reveals the intricate molecular interactions and a plausible switching mechanism for the hook to be flexible in bending but rigid against twisting for its universal joint function.

PubMed: 15510139
DOI: 10.1038/nature02997

実験手法

X-RAY DIFFRACTION (1.8 Å)