Protein Family Models

This domain is found at the N-terminus of the chaperone SurA and related proteins such as PpiD and foldase PrsA [1,2]. It is a helical domain that together with the C-terminal, forms a domain containing substrate-binding sites [2,3]. The C-terminal of the SurA protein folds back and forms part of this domain also but is not included in the current alignment. [1]. 12429090. Crystallographic structure of SurA, a molecular chaperone that. facilitates folding of outer membrane porins.. Bitto E, McKay DB;. Structure. 2002;10:1489-1498.. [2]. 20970503. The crystal structure of the leptospiral hypothetical protein. LIC12922 reveals homology with the periplasmic chaperone SurA.. Giuseppe PO, Von Atzingen M, Nascimento AL, Zanchin NI,. Guimaraes BG;. J Struct Biol. 2011;173:312-322.. [3]. 32358557. 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. 2020;11:2155. (from Pfam)

Date:

2024-04-03

Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline. (from Pfam)

Date:

2023-12-12

Date:

2023-12-12

Rotamases increase the rate of protein folding by catalysing the interconversion of cis-proline and trans-proline. (from Pfam)

Date:

2023-12-12