3GU0

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

Summary for 3GU0

• Entry DOI: 10.2210/pdb3gu0/pdb
• Related: 2NSA 2NSB 2NSC 3GTY
• Descriptor: Trigger factor (1 entity in total)
• Functional Keywords: molecular chaperone, cell cycle, cell division, chaperone, isomerase, rotamase
• Biological source: Thermotoga maritima
• Cellular location: Cytoplasm: Q9WZF8
• Total number of polymer chains: 1
• Total formula weight: 48790.41

Authors

Martinez-Hackert, E.,Hendrickson, W.A. (deposition date: 2009-03-28, release date: 2009-12-22, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.5 Å)