SSF109998

Triger factor/SurA peptide-binding domain-like

SUPERFAMILY entry
Member databaseSUPERFAMILY
SUPERFAMILY typehomologous superfamily

Description
Imported from IPR027304

The C-terminal domain of trigger factor and the peptide-binding domain of porin chaperone SurA share a multi-helical structure consisting of an irregular array of long and short helices.

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 domain which mediates association with the large ribosomal subunit, a central PPIase domain with homology to FKBP proteins, and a C-terminal substrate-binding domain
[1, 3]
. 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, 3]
.

The porin chaperon SurA facilitates correct folding of outer membrane proteins in Gram-negative bacteria
[2, 4]
.

References
Imported from IPR027304

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.Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Bitto E, McKay DB. Structure 10, 1489-98, (2002). View articlePMID: 12429090

3.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

4.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

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