6CH2

Crystal structure of the cytoplasmic domain of FlhA and FliT-FliD complex

6CH2 の概要

• エントリーDOI: 10.2210/pdb6ch2/pdb
• 分子名称: Flagellar biosynthesis protein FlhA, Flagellar hook-associated protein 2,Flagellar protein FliT, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: flagellar, structural protein
• 由来する生物種: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 169070.18

構造登録者

Xing, Q.,Shi, K.,Kalodimos, C.G. (登録日: 2018-02-21, 公開日: 2018-05-16, 最終更新日: 2023-10-04)

主引用文献

Xing, Q.,Shi, K.,Portaliou, A.,Rossi, P.,Economou, A.,Kalodimos, C.G.
Structures of chaperone-substrate complexes docked onto the export gate in a type III secretion system.
Nat Commun, 9:1773-1773, 2018

PubMed Abstract: The flagellum and the injectisome enable bacterial locomotion and pathogenesis, respectively. These nanomachines assemble and function using a type III secretion system (T3SS). Exported proteins are delivered to the export apparatus by dedicated cytoplasmic chaperones for their transport through the membrane. The structural and mechanistic basis of this process is poorly understood. Here we report the structures of two ternary complexes among flagellar chaperones (FliT and FliS), protein substrates (the filament-capping FliD and flagellin FliC), and the export gate platform protein FlhA. The substrates do not interact directly with FlhA; however, they are required to induce a binding-competent conformation to the chaperone that exposes the recognition motif featuring a highly conserved sequence recognized by FlhA. The structural data reveal the recognition signal in a class of T3SS proteins and provide new insight into the assembly of key protein complexes at the export gate.

PubMed: 29720631
DOI: 10.1038/s41467-018-04137-4

実験手法

X-RAY DIFFRACTION (2.7 Å)