3t1u | pdb_00003t1u

Crystal Structure of the complex of Cyclophilin-A enzyme from Azotobacter vinelandii with sucAFPFpNA peptide

spinqualitylabelsall models 3t1u, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3t1u is a 2 chain structure with sequence from Azovd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: NIT, SIN Related: 3t17 Gene: Avin_23510 (AZOVD) Activity: Peptidylprolyl isomerase, with EC number 5.2.1.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cyclophilin 3D structures

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