2NSC

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

Summary for 2NSC

• Entry DOI: 10.2210/pdb2nsc/pdb
• Related: 2nsa 2nsb
• Descriptor: Trigger factor (2 entities in total)
• Functional Keywords: chaperone
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm: Q9WZF8
• Total number of polymer chains: 1
• Total formula weight: 12818.84

Authors

Martinez-Hackert, E.,Hendrickson, W.A. (deposition date: 2006-11-03, release date: 2007-03-27, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)