5FHY

Crystal structure of FliD (HAP2) from Pseudomonas aeruginosa PAO1

5FHY の概要

• エントリーDOI: 10.2210/pdb5fhy/pdb
• 分子名称: B-type flagellar hook-associated protein 2, SODIUM ION (3 entities in total)
• 機能のキーワード: bacterial flagella, cap protein, structural protein
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
• 細胞内の位置: Secreted: Q9K3C5
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71820.44

構造登録者

Postel, S.,Bonsor, D.,Diederichs, K.,Sundberg, E.J. (登録日: 2015-12-22, 公開日: 2016-10-05, 最終更新日: 2024-04-03)

主引用文献

Postel, S.,Deredge, D.,Bonsor, D.A.,Yu, X.,Diederichs, K.,Helmsing, S.,Vromen, A.,Friedler, A.,Hust, M.,Egelman, E.H.,Beckett, D.,Wintrode, P.L.,Sundberg, E.J.
Bacterial flagellar capping proteins adopt diverse oligomeric states.
Elife, 5:-, 2016

PubMed Abstract: Flagella are crucial for bacterial motility and pathogenesis. The flagellar capping protein (FliD) regulates filament assembly by chaperoning and sorting flagellin (FliC) proteins after they traverse the hollow filament and exit the growing flagellum tip. In the absence of FliD, flagella are not formed, resulting in impaired motility and infectivity. Here, we report the 2.2 Å resolution X-ray crystal structure of FliD from , the first high-resolution structure of any FliD protein from any bacterium. Using this evidence in combination with a multitude of biophysical and functional analyses, we find that FliD exhibits unexpected structural similarity to other flagellar proteins at the domain level, adopts a unique hexameric oligomeric state, and depends on flexible determinants for oligomerization. Considering that the flagellin filaments on which FliD oligomers are affixed vary in protofilament number between bacteria, our results suggest that FliD oligomer stoichiometries vary across bacteria to complement their filament assemblies.

PubMed: 27664419
DOI: 10.7554/eLife.18857

実験手法

X-RAY DIFFRACTION (2.201 Å)