3SQB

Structure of the major type 1 pilus subunit FimA bound to the FimC chaperone

3SQB の概要

• エントリーDOI: 10.2210/pdb3sqb/pdb
• 関連するPDBエントリー: 2jty 4DWH
• 分子名称: Chaperone protein fimC, Type-1 fimbrial protein, A chain, DI(HYDROXYETHYL)ETHER, ... (6 entities in total)
• 機能のキーワード: immunoglobin-like fold, involved in type 1 pilus assembly, structural protein-chaperone complex, structural protein/chaperone
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Periplasm: P31697; Fimbrium: P04128
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 156529.18

構造登録者

Scharer, M.A.,Eidam, O.,Grutter, M.G.,Glockshuber, R.,Capitani, G. (登録日: 2011-07-05, 公開日: 2012-05-30, 最終更新日: 2024-10-30)

主引用文献

Crespo, M.D.,Puorger, C.,Scharer, M.A.,Eidam, O.,Grutter, M.G.,Capitani, G.,Glockshuber, R.
Quality control of disulfide bond formation in pilus subunits by the chaperone FimC.
Nat.Chem.Biol., 8:707-713, 2012

PubMed Abstract: Type 1 pili from uropathogenic Escherichia coli are filamentous, noncovalent protein complexes mediating bacterial adhesion to the host tissue. All structural pilus subunits are homologous proteins sharing an invariant disulfide bridge. Here we show that disulfide bond formation in the unfolded subunits, catalyzed by the periplasmic oxidoreductase DsbA, is required for subunit recognition by the assembly chaperone FimC and for FimC-catalyzed subunit folding. FimC thus guarantees quantitative disulfide bond formation in each of the up to 3,000 subunits of the pilus. The X-ray structure of the complex between FimC and the main pilus subunit FimA and the kinetics of FimC-catalyzed FimA folding indicate that FimC accelerates folding of pilus subunits by lowering their topological complexity. The kinetic data, together with the measured in vivo concentrations of DsbA and FimC, predict an in vivo half-life of 2 s for oxidative folding of FimA in the periplasm.

PubMed: 22772153
DOI: 10.1038/nchembio.1019

実験手法

X-RAY DIFFRACTION (3.2 Å)