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Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor ChaperonePromiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone
Structural highlights
Function[TIG_THEMA] Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTrigger 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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