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3t1u, resolution 2.00Å ()
Non-Standard Residues: ,
Gene: Avin_23510 (Azotobacter vinelandii DJ)
Activity: Peptidylprolyl isomerase, with EC number
Related: 3t17

Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml

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

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.

About this Structure

3t1u is a 2 chain structure with sequence from Azotobacter vinelandii dj. Full crystallographic information is available from OCA.

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