3T1U

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

Summary for 3T1U

Entry DOI	10.2210/pdb3t1u/pdb
Related	3T17
Descriptor	Peptidyl-prolyl cis-trans isomerase, succinyl-Ala-Phe-Pro-Phe-p-nitroanilide (3 entities in total)
Functional Keywords	peptidyl-prolyl isomerase, ppiase, isomerase
Biological source	Azotobacter vinelandii
Total number of polymer chains	2
Total formula weight	18382.53
Authors	Karpusas, M.,Christoforides, E.,Bethanis, K.,Dimou, M.,Katinakis, P. (deposition date: 2011-07-22, release date: 2012-03-07, Last modification date: 2023-09-13)
Primary citation	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, 68:259-264, 2012 Cited by PubMed Abstract: 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. PubMed: 22442217 DOI: 10.1107/S1744309112000188 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation