Structural highlights
Function
[C1DHE4_AZOVD] PPIases accelerate the folding of proteins. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223]
Publication Abstract from PubMed
Cyclophilins constitute a class of peptidyl-prolyl isomerases which participate in processes related to protein folding, signalling and chaperoning. The crystal structure of the cytoplasmic cyclophilin A (CyPA) from the bacterium Azotobacter vinelandii complexed with a synthetic tetrapeptide was determined by molecular replacement at 2 resolution. The proline in the tetrapeptide is observed to adopt the cis-isomer conformation. Comparisons of this structure with other CyPA structures provide insights into the conformational variability, effects of peptide binding and structure-function relationships of this enzyme.
Structure of a bacterial cytoplasmic cyclophilin A in complex with a tetrapeptide.,Christoforides E, Dimou M, Katinakis P, Bethanis K, Karpusas M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Mar 1;68(Pt 3):259-64., Epub 2012 Feb 15. PMID:22442217[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Christoforides E, Dimou M, Katinakis P, Bethanis K, Karpusas M. Structure of a bacterial cytoplasmic cyclophilin A in complex with a tetrapeptide. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Mar 1;68(Pt 3):259-64., Epub 2012 Feb 15. PMID:22442217 doi:http://dx.doi.org/10.1107/S1744309112000188
