3T1U

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

3T1U の概要

• エントリーDOI: 10.2210/pdb3t1u/pdb
• 関連するPDBエントリー: 3T17
• 分子名称: Peptidyl-prolyl cis-trans isomerase, succinyl-Ala-Phe-Pro-Phe-p-nitroanilide (3 entities in total)
• 機能のキーワード: peptidyl-prolyl isomerase, ppiase, isomerase
• 由来する生物種: Azotobacter vinelandii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18382.53

構造登録者

Karpusas, M.,Christoforides, E.,Bethanis, K.,Dimou, M.,Katinakis, P. (登録日: 2011-07-22, 公開日: 2012-03-07, 最終更新日: 2023-09-13)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (2 Å)