Dynamic properties of the first enzymatic reaction steps of porcine pancreatic elastase. How rigid is the active site of the native enzyme? Molecular dynamics simulation
| Autor: | Gail Carlson‐Golab, Stanley M. Swanson, Maciej Geller, Edgar F. Meyer, Bogdan Lesyng |
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| Rok vydání: | 1990 |
| Předmět: |
Binding Sites
Pancreatic Elastase biology Protein Conformation Swine Chemistry Hydrogen bond Stereochemistry Organic Chemistry Biophysics Substrate (chemistry) Active site Hydrogen Bonding General Medicine Biochemistry Biomaterials Molecular dynamics Protein structure Side chain biology.protein Animals Computer Simulation Binding site Pancreatic elastase |
| Zdroj: | Biopolymers. 30:781-796 |
| ISSN: | 1097-0282 0006-3525 |
| DOI: | 10.1002/bip.360300713 |
| Popis: | Two molecular dynamics simulations (100 and 50 ps) of native porcine pancreatic elastase i.e., without bound substrate and with the active site hydrated by a dome of water (630 molecules) have been performed. Dynamical properties of the catalytic tetrad have been examined. While relative conformations of the Asp 102, His 57, and Ser 214 are rather stable in time, the side chain of Ser 195 undergoes several conformational changes. No preferences are observed for the formation of a hydrogen bond between the O gamma-H group (Ser 195) and nitrogen N, (His 57). A cluster of ordered water molecules effectively competes with the H-O gamma group (Ser 195) and thereby prevents the formation of this H bond, which is generally agreed to be crucial for catalysis. |
| Databáze: | OpenAIRE |
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