6JYM

Crystal structure of Prolyl Endopeptidase from Haliotis discus hannai

6JYM の概要

• エントリーDOI: 10.2210/pdb6jym/pdb
• 分子名称: Prolyl endopeptidase (2 entities in total)
• 機能のキーワード: a serine protease subfamily, hydrolase
• 由来する生物種: Haliotis discus hannai (Japanese abalone)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 85880.13

構造登録者

Li, W.,Cao, M.,Jin, T. (登録日: 2019-04-26, 公開日: 2020-04-29, 最終更新日: 2023-11-22)

主引用文献

Li, W.Y.,Li, Y.,Chen, Y.L.,Hu, J.J.,Mengist, H.M.,Liu, G.M.,Jin, T.,Cao, M.J.
Characterization and crystal structure of prolyl endopeptidase from abalone (Haliotis discus hannai).
FOOD CHEM, 333:127452-127452, 2020

PubMed Abstract: Aimed to study the characteristics of prolyl endopeptidase (PEP, EC 3.4.21.26) and its possible role in the degradation of collagen, we cloned the full-length cDNA sequence of PEP from abalone (Haliotis discus hannai) (Hdh-PEP). Recombinant Hdh-PEP (rHdh-PEP) was expressed in vitro, its enzymatic properties were detected, and its secondary structure was analyzed by Circular Dichroism (CD). We for the first time determined the 1.5 Å crystal structure of rHdh-PEP. The decomposition effect of rHdh-PEP on collagen peptides was analyzed. Our data revealed that the molecular weight of rHdh-PEP is 85 kDa, consisting of a catalytic domain and a β-propeller domain. The optimal pH and temperature of rHdh-PEP were pH 6.0 and 20 °C, respectively. Using small collagen peptides as substrates, HPLC-ESI-MS analysis confirmed that rHdh-PEP specifically cleaved at the carboxyl side of proline residues, suggesting its role in the degradation of collagen peptides during autolysis.

PubMed: 32673951
DOI: 10.1016/j.foodchem.2020.127452

実験手法

X-RAY DIFFRACTION (1.5 Å)