6AI2

Structure of the 328-692 fragment of FlhA (F459A)

6AI2 の概要

• エントリーDOI: 10.2210/pdb6ai2/pdb
• 関連するPDBエントリー: 3A5I
• 分子名称: Flagellar biosynthesis protein FlhA (1 entity in total)
• 機能のキーワード: flagellar type iii secretion, protein transport
• 由来する生物種: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81191.09

構造登録者

Ogawa, Y.,Kinoshita, M.,Minamino, T.,Imada, K. (登録日: 2018-08-21, 公開日: 2019-03-20, 最終更新日: 2023-11-22)

主引用文献

Inoue, Y.,Ogawa, Y.,Kinoshita, M.,Terahara, N.,Shimada, M.,Kodera, N.,Ando, T.,Namba, K.,Kitao, A.,Imada, K.,Minamino, T.
Structural Insights into the Substrate Specificity Switch Mechanism of the Type III Protein Export Apparatus.
Structure, 27:965-, 2019

PubMed Abstract: Bacteria use a type III protein export apparatus for construction of the flagellum, which consists of the basal body, the hook, and the filament. FlhA forms a homo-nonamer through its C-terminal cytoplasmic domains (FlhA) and ensures the strict order of flagellar assembly. FlhA goes through dynamic domain motions during protein export, but it remains unknown how it occurs. Here, we report that the FlhA(G368C) mutation biases FlhA toward a closed form, thereby reducing the binding affinity of FlhA for flagellar export chaperones in complex with their cognate filament-type substrates. The G368C mutations also restrict the conformational flexibility of a linker region of FlhA (FlhA), suppressing FlhA ring formation. We propose that interactions of FlhA with its neighboring subunit converts FlhA in the ring from a closed conformation to an open one, allowing the chaperon/substrate complexes to bind to the FlhA ring to form the filament at the hook tip.

PubMed: 31031200
DOI: 10.1016/j.str.2019.03.017

実験手法

X-RAY DIFFRACTION (3.3 Å)