D
IPR008880

Trigger factor, C-terminal

InterPro entry
Short nameTrigger_fac_C
Overlapping
homologous
superfamilies
 

Description

In the Escherichia coli cytosol, a fraction of the newly synthesised proteins requires the activity of molecular chaperones for folding to the native state. The major chaperones implicated in this folding process are the ribosome-associated Trigger Factor (TF), and the DnaK and GroEL chaperones with their respective co-chaperones. Trigger Factor is an ATP-independent chaperone and displays chaperone and peptidyl-prolyl-cis-trans-isomerase (PPIase) activitiesin vitro. It is composed of three domains, an N-terminal ribosome-binding domain (RBD) which mediates association with the large ribosomal subunit, a central PPIase domain with homology to FKBP proteins, and a C-terminal substrate-binding domain (SBD) which forms the central body of the protein and has two helical arms that create a cavity
[2]
. The association between its N-terminal domain with the ribosomal protein L23 located next to the peptide tunnel exit is essential for the interaction with nascent polypeptides and its in vivo function
[1]
.

This entry represents the C-terminal domain of bacterial TF proteins, which has a multi-helical structure consisting of an irregular array of long and short helices. This domain is structurally similar to the peptide-binding domain of the bacterial porin chaperone SurA
[3]
.

References

1.Trigger Factor and DnaK possess overlapping substrate pools and binding specificities. Deuerling E, Patzelt H, Vorderwulbecke S, Rauch T, Kramer G, Schaffitzel E, Mogk A, Schulze-Specking A, Langen H, Bukau B. Mol. Microbiol. 47, 1317-28, (2003). View articlePMID: 12603737

2.The dynamic dimer structure of the chaperone Trigger Factor. Morgado L, Burmann BM, Sharpe T, Mazur A, Hiller S. Nat Commun 8, 1992, (2017). PMID: 29222465

3.Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients. Calabrese AN, Schiffrin B, Watson M, Karamanos TK, Walko M, Humes JR, Horne JE, White P, Wilson AJ, Kalli AC, Tuma R, Ashcroft AE, Brockwell DJ, Radford SE. Nat Commun 11, 2155, (2020). PMID: 32358557

GO terms

molecular function

  • None

cellular component

  • None

Cross References

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