2MLX

NMR structure of E. coli Trigger Factor in complex with unfolded PhoA220-310

2MLX の概要

• エントリーDOI: 10.2210/pdb2mlx/pdb
• 関連するPDBエントリー: 2mly 2mlz
• NMR情報: BMRB: 19835
• 分子名称: Trigger factor, Alkaline phosphatase (2 entities in total)
• 機能のキーワード: molecular chaperone, unfolded protein, protein complex, chaperone
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm: U6N3P1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59562.24

構造登録者

Saio, T.,Guan, X.,Rossi, P.,Economou, A.,Kalodimos, C.G. (登録日: 2014-03-05, 公開日: 2014-05-21, 最終更新日: 2024-05-01)

主引用文献

Saio, T.,Guan, X.,Rossi, P.,Economou, A.,Kalodimos, C.G.
Structural basis for protein antiaggregation activity of the trigger factor chaperone.
Science, 344:1250494-1250494, 2014

PubMed Abstract: Molecular chaperones prevent aggregation and misfolding of proteins, but scarcity of structural data has impeded an understanding of the recognition and antiaggregation mechanisms. We report the solution structure, dynamics, and energetics of three trigger factor (TF) chaperone molecules in complex with alkaline phosphatase (PhoA) captured in the unfolded state. Our data show that TF uses multiple sites to bind to several regions of the PhoA substrate protein primarily through hydrophobic contacts. Nuclear magnetic resonance (NMR) relaxation experiments show that TF interacts with PhoA in a highly dynamic fashion, but as the number and length of the PhoA regions engaged by TF increase, a more stable complex gradually emerges. Multivalent binding keeps the substrate protein in an extended, unfolded conformation. The results show how molecular chaperones recognize unfolded polypeptides and, by acting as unfoldases and holdases, prevent the aggregation and premature (mis)folding of unfolded proteins.

PubMed: 24812405
DOI: 10.1126/science.1250494

実験手法

SOLUTION NMR