Summary for 7FFP
| Entry DOI | 10.2210/pdb7ffp/pdb |
| Related | 7C9B |
| Descriptor | Alpha-aspartyl dipeptidase, ASPARTIC ACID, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | peptidase-e, aspartyl dipeptidase, alpha-aspartyl dipeptidase, hydrolase |
| Biological source | Xenopus laevis (African clawed frog) |
| Total number of polymer chains | 1 |
| Total formula weight | 27163.99 |
| Authors | Kumar, A.,Singh, R.,Makde, R.D. (deposition date: 2021-07-23, release date: 2021-09-08, Last modification date: 2023-11-29) |
| Primary citation | Kumar, A.,Singh, R.,Ghosh, B.,Makde, R.D. Crystal structure of aspartyl dipeptidase from Xenopus laevis revealed ligand binding induced loop ordering and catalytic triad assembly. Proteins, 90:299-308, 2022 Cited by PubMed Abstract: Gene encoding aspartyl dipeptidase from Xenopus levies (PepExl) is upregulated by thyroid hormone and is proposed to play a significant role in resorption of tadpole tail during metamorphosis. However, the importance of peptidase activity for the resorption of the tail remain elusive. Here we report the crystal structures of first eukaryotic S51 peptidase, PepExl, in its ligand-free and Asp-bound states at 1.4 and 1.8 Å resolutions, respectively. The active site is located at dimeric interface and the catalytic triad is found to be dissembled in ligand-free and assembled in Asp-bound state. Structural comparison and molecular dynamic simulations of ligand-free and Asp-bound states shows that distinct loop (loop-A) plays an important role in active site shielding, substrate binding and enzyme activation. This study illuminates the Asp-X dipeptide binding in PepExl is associated with ordering of the loop-A and assembly of residues of catalytic triad in active conformation for enzymatic activity. PubMed: 34431561DOI: 10.1002/prot.26220 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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