2NSA

Structures of and interactions between domains of trigger factor from Themotoga maritim

2NSA の概要

• エントリーDOI: 10.2210/pdb2nsa/pdb
• 分子名称: Trigger factor, SULFATE ION (3 entities in total)
• 機能のキーワード: chaperone
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20740.08

構造登録者

Martinez-Hackert, E.,Hendrickson, W.A. (登録日: 2006-11-03, 公開日: 2007-03-27, 最終更新日: 2024-11-20)

主引用文献

Martinez-Hackert, E.,Hendrickson, W.A.
Structures of and interactions between domains of trigger factor from Thermotoga maritima.
Acta Crystallogr.,Sect.D, 63:536-547, 2007

PubMed Abstract: Trigger factor (TF) is a eubacterial chaperone that associates with ribosomes at the peptide-exit tunnel and also occurs in excess free in the cytosol. TF is a three-domain protein that appears to exist in a dynamic equilibrium of oligomerization states and interdomain conformations. X-ray crystallography and chemical cross-linking were used to study the roles of the N- and C-terminal domains of Thermotoga maritima TF in TF oligomerization and chaperone activity. The structural conservation of both the N- and C-terminal TF domains was unambiguously established. The biochemical and crystallographic data reveal a tendency for these domains to partake in diverse and apparently nonspecific protein-protein interactions. It is found that the T. maritima and Escherichia coli TF surfaces lack evident exposed hydrophobic patches. Taken together, these data suggest that TF chaperones could interact with nascent proteins via hydrophilic surfaces.

PubMed: 17372359
DOI: 10.1107/S090744490700964X

実験手法

X-RAY DIFFRACTION (1.7 Å)