7CTN

Structure of the 328-692 fragment of FlhA (E351A/D356A)

7CTN の概要

• エントリーDOI: 10.2210/pdb7ctn/pdb
• 関連するPDBエントリー: 3A5I 6AI0
• 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: 81317.38

構造登録者

Kida, M.,Takekawa, N.,Kinoshita, M.,Inoue, Y.,Minamino, T.,Imada, K. (登録日: 2020-08-19, 公開日: 2021-04-28, 最終更新日: 2023-11-29)

主引用文献

Inoue, Y.,Kinoshita, M.,Kida, M.,Takekawa, N.,Namba, K.,Imada, K.,Minamino, T.
The FlhA linker mediates flagellar protein export switching during flagellar assembly.
Commun Biol, 4:646-646, 2021

PubMed Abstract: The flagellar protein export apparatus switches substrate specificity from hook-type to filament-type upon hook assembly completion, thereby initiating filament assembly at the hook tip. The C-terminal cytoplasmic domain of FlhA (FlhA) serves as a docking platform for flagellar chaperones in complex with their cognate filament-type substrates. Interactions of the flexible linker of FlhA (FlhA) with its nearest FlhA subunit in the FlhA ring is required for the substrate specificity switching. To address how FlhA brings the order to flagellar assembly, we analyzed the flhA(E351A/W354A/D356A) ΔflgM mutant and found that this triple mutation in FlhA increased the secretion level of hook protein by 5-fold, thereby increasing hook length. The crystal structure of FlhA(E351A/D356A) showed that FlhA bound to the chaperone-binding site of its neighboring subunit. We propose that the interaction of FlhA with the chaperon-binding site of FlhA suppresses filament-type protein export and facilitates hook-type protein export during hook assembly.

PubMed: 34059784
DOI: 10.1038/s42003-021-02177-z

実験手法

X-RAY DIFFRACTION (2.8 Å)