6JYM
Crystal structure of Prolyl Endopeptidase from Haliotis discus hannai
Summary for 6JYM
| Entry DOI | 10.2210/pdb6jym/pdb |
| Descriptor | Prolyl endopeptidase (2 entities in total) |
| Functional Keywords | a serine protease subfamily, hydrolase |
| Biological source | Haliotis discus hannai (Japanese abalone) |
| Total number of polymer chains | 1 |
| Total formula weight | 85880.13 |
| Authors | |
| Primary citation | 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 Cited by 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: 32673951DOI: 10.1016/j.foodchem.2020.127452 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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