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3gu0, resolution 3.50Å ()
Gene: tig, TM_0694 (Thermotoga maritima)
Related: 2nsc, 2nsb, 2nsa, 3gty
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml

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

Publication Abstract from PubMed

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.

Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone., Martinez-Hackert E, Hendrickson WA, Cell. 2009 Sep 4;138(5):923-34. PMID:19737520

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

3gu0 is a 1 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA.


  • Martinez-Hackert E, Hendrickson WA. Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone. Cell. 2009 Sep 4;138(5):923-34. PMID:19737520 doi:10.1016/j.cell.2009.07.044

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