3GTY

Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone

3GTY の概要

• エントリーDOI: 10.2210/pdb3gty/pdb
• 関連するPDBエントリー: 2NSA 2NSB 2NSC 3GU0
• 分子名称: Trigger factor, 30S ribosomal protein S7 (2 entities in total)
• 機能のキーワード: chaperone-client complex, cell cycle, cell division, chaperone, isomerase, rotamase, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, chaperone-ribosomal protein complex, chaperone/ribosomal protein
• 由来する生物種: Thermotoga maritima; 詳細
• 細胞内の位置: Cytoplasm: Q9WZF8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68172.86

構造登録者

Martinez-Hackert, E.,Hendrickson, W.A. (登録日: 2009-03-28, 公開日: 2009-12-22, 最終更新日: 2024-02-21)

主引用文献

Martinez-Hackert, E.,Hendrickson, W.A.
Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone
Cell(Cambridge,Mass.), 138:923-934, 2009

PubMed Abstract: Trigger factor (TF) is a molecular chaperone that binds to bacterial ribosomes where it contacts emerging nascent chains, but TF is also abundant free in the cytosol where its activity is less well characterized. In vitro studies show that TF promotes protein refolding. We find here that ribosome-free TF stably associates with and rescues from misfolding a large repertoire of full-length proteins. We identify over 170 members of this cytosolic Escherichia coli TF substrate proteome, including ribosomal protein S7. We analyzed the biochemical properties of a TF:S7 complex from Thermotoga maritima and determined its crystal structure. Thereby, we obtained an atomic-level picture of a promiscuous chaperone in complex with a physiological substrate protein. The structure of the complex reveals the molecular basis of substrate recognition by TF, indicates how TF could accelerate protein folding, and suggests a role for TF in the biogenesis of protein complexes.

PubMed: 19737520
DOI: 10.1016/j.cell.2009.07.044

実験手法

X-RAY DIFFRACTION (3.4 Å)