8JCR
Crystal structure of Calotropain FI from Calotropis gigantea (pH 6.0)
Summary for 8JCR
| Entry DOI | 10.2210/pdb8jcr/pdb |
| Related | 8JCQ |
| Descriptor | Procerain, Calotropain FI, GLYCEROL, N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE, ... (4 entities in total) |
| Functional Keywords | plant protease, cystein peptidase, latex, calotropis gigantea, hydrolase, endopeptidase |
| Biological source | Calotropis gigantea |
| Total number of polymer chains | 1 |
| Total formula weight | 23883.39 |
| Authors | Kumar, A.,Jamdar, S.N.,Srivastava, G.,Makde, R.D. (deposition date: 2023-05-11, release date: 2024-05-22, Last modification date: 2025-03-19) |
| Primary citation | Jamdar, S.N.,Kumar, A.,Srivastava, G.,Makde, R.D. Crystal Structure of Papain-Like Cysteine Protease, Calotropain FI, Purified from the Latex of Calotropis gigantea. J.Agric.Food Chem., 2025 Cited by PubMed Abstract: The latex of and elute as two distinct peaks on cation exchange chromatography. One of the peaks is reported to possess multiple papain-like cysteine proteases with different biochemical properties that have been identified with different names. This is mainly due to the absence of a primary sequence for the proteases. Here, we report the crystal structures of calotropain FI from bound to the inhibitor E64 at pH 6 and 9 at 1.25 and 1.4 Å, respectively. Both structures are identical and are very similar to ervatamin B and papain structures. The high quality of electron density maps revealed the primary sequence of calotropain FI. The sequence comparison shows that calotropain FI from is orthologous to procerain, CpCp1-3, and SnuCalCp03 from and rather distinct from procerain B. PubMed: 40036158DOI: 10.1021/acs.jafc.4c10898 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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