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|3t1u, resolution 2.00Å ()|
|Gene:||Avin_23510 (Azotobacter vinelandii DJ)|
Crystal Structure of the complex of Cyclophilin-A enzyme from Azotobacter vinelandii with sucAFPFpNA peptide
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.