Member database | CATH-Gene3D |
CATH-Gene3D type | homologous superfamily |
Description Imported from IPR046357
References Imported from IPR046357
1.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
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.NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein. Vogtherr M, Jacobs DM, Parac TN, Maurer M, Pahl A, Saxena K, Ruterjans H, Griesinger C, Fiebig KM. J. Mol. Biol. 318, 1097-115, (2002). View articlePMID: 12054805
4.Solution structure of Escherichia coli Par10: The prototypic member of the Parvulin family of peptidyl-prolyl cis/trans isomerases. Kuhlewein A, Voll G, Hernandez Alvarez B, Kessler H, Fischer G, Rahfeld JU, Gemmecker G. Protein Sci. 13, 2378-87, (2004). View articlePMID: 15322281
5.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
6.Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins. Ferbitz L, Maier T, Patzelt H, Bukau B, Deuerling E, Ban N. Nature 431, 590-6, (2004). View articlePMID: 15334087
7.Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis. Vitikainen M, Lappalainen I, Seppala R, Antelmann H, Boer H, Taira S, Savilahti H, Hecker M, Vihinen M, Sarvas M, Kontinen VP. J. Biol. Chem. 279, 19302-14, (2004). View articlePMID: 14976191
8.Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. Saul FA, Arie JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA. J. Mol. Biol. 335, 595-608, (2004). View articlePMID: 14672666