2nsb
From Proteopedia
Structures of and interactions between domains of trigger factor from Themotoga maritima
Overview
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.
About this Structure
2NSB is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Structures of and interactions between domains of trigger factor from Thermotoga maritima., Martinez-Hackert E, Hendrickson WA, Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):536-47. Epub 2007, Mar 16. PMID:17372359 Page seeded by OCA on Thu May 22 22:26:11 2008
