Cutting at the right place. The importance of selective limited proteolysis in the activation of proproteinase E
| Autor: | Salvador Ventura, F.X. Gomis-Ruth, Wolfram Bode, Mariola Gomez-Ortiz, Josep Vendrell, Francesc X. Avilés, Robert Huber |
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| Rok vydání: | 1998 |
| Předmět: |
Models
Molecular Carboxypeptidases A Macromolecular Substances Protein Conformation Swine Molecular Sequence Data Chymotrypsinogen Carboxypeptidases Crystallography X-Ray Biochemistry Protein structure Zymogen Endopeptidases Animals Humans Amino Acid Sequence Pancreas Pancreatic elastase Ternary complex Serine protease Enzyme Precursors Pancreatic Elastase biology Chemistry Serine Endopeptidases Proteolytic enzymes Carboxypeptidase Enzyme Activation biology.protein Cattle Sequence Alignment |
| Zdroj: | European Journal of Biochemistry. 251:839-844 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1046/j.1432-1327.1998.2510839.x |
| Popis: | Proteinase E is a proteolytic enzyme which belongs to a distinct subfamily of chymotrypsin-like serine endopeptidases. Its proform from the bovine pancreatic system has been structurally analyzed by X-ray crystallography for the intact native form, with a 11-residue N-terminal activation peptide, in a ternary complex with chymotrypsinogen C and procarboxypeptidase A [Gomis-Ruth, F. X., Gomez, M., Bode, W., Huber, R. & Aviles, F. X. (1995) The three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen C, EMBO J. 14, 4387-4394]. Also for a N-terminally truncated form, lacking the first 13 residues and called subunit III, a crystal structure is available [Pignol, D., Gaboriaud, C., Michon, T., Kerfelec, B., Chapus, C. & Fontecilla-Camps, J. C. (1994) Crystal structure of bovine procarboxypeptidase A-S6 subunit III, a highly structured truncated zymogen E, EMBO J. 8, 1763-1771]. Both structures are well defined by electron density, except for the first 7 residues of subunit III. However, both structures present large deviations of up to 2 nm in several regions, indicating that they correspond to two quite distinct states of low free energy, influenced by very few contacts made via the N-terminal segment. As no structure of an active proteinase E is known so far, pancreatic porcine elastase has been chosen as a model for this enzyme and an activation mechanism for this distinct serine endopeptidase subfamily is proposed. |
| Databáze: | OpenAIRE |
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