5WRH

FlgG structure based on the CryoEM map of the bacterial flagellar polyrod

5WRH の概要

• エントリーDOI: 10.2210/pdb5wrh/pdb
• EMDBエントリー: 6683
• 分子名称: Flagellar basal-body rod protein FlgG (1 entity in total)
• 機能のキーワード: the bacterial flagellar motor, motor protein
• 由来する生物種: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
• 細胞内の位置: Bacterial flagellum basal body: P0A1J3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27784.81

構造登録者

Fujii, T.,Namba, K. (登録日: 2016-12-02, 公開日: 2017-02-08, 最終更新日: 2024-10-09)

主引用文献

Fujii, T.,Kato, T.,Hiraoka, K.D.,Miyata, T.,Minamino, T.,Chevance, F.F.,Hughes, K.T.,Namba, K.
Identical folds used for distinct mechanical functions of the bacterial flagellar rod and hook.
Nat Commun, 8:14276-14276, 2017

PubMed Abstract: The bacterial flagellum is a motile organelle driven by a rotary motor, and its axial portions function as a drive shaft (rod), a universal joint (hook) and a helical propeller (filament). The rod and hook are directly connected to each other, with their subunit proteins FlgG and FlgE having 39% sequence identity, but show distinct mechanical properties; the rod is straight and rigid as a drive shaft whereas the hook is flexible in bending as a universal joint. Here we report the structure of the rod and comparison with that of the hook. While these two structures have the same helical symmetry and repeat distance and nearly identical folds of corresponding domains, the domain orientations differ by ∼7°, resulting in tight and loose axial subunit packing in the rod and hook, respectively, conferring the rigidity on the rod and flexibility on the hook. This provides a good example of versatile use of a protein structure in biological organisms.

PubMed: 28120828
DOI: 10.1038/ncomms14276

実験手法

ELECTRON MICROSCOPY (7.4 Å)