Crystal structures of wild-type Trichoderma reesei Cel7A catalytic domain in open and closed states
| Autor: | Annette M. Bodenheimer, Flora Meilleur |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Glycoside Hydrolases Biophysics Crystal structure Molecular Dynamics Simulation Crystallography X-Ray Biochemistry 03 medical and health sciences Molecular dynamics Structural Biology Catalytic Domain Hydrolase Genetics Binding site Molecular Biology Trichoderma reesei Trichoderma Binding Sites biology Chemistry Wild type Cell Biology Processivity biology.organism_classification Crystallography 030104 developmental biology Product inhibition Mutation |
| Zdroj: | FEBS letters. 590(23) |
| ISSN: | 1873-3468 |
| Popis: | Trichoderma reesei Cel7A efficiently hydrolyses cellulose. We report here the crystallographic structures of the wild-type TrCel7A catalytic domain (CD) in an open state and, for the first time, in a closed state. Molecular dynamics (MD) simulations indicate that the loops along the CD tunnel move in concerted motions. Together the crystallographic and MD data suggest that the CD cycles between the tense and relaxed forms that are characteristic of work producing enzymes. Analysis of the interactions formed by R251 provides a structural rationale for the concurrent decrease in product inhibition and catalytic efficiency measured for product binding site mutants. This article is protected by copyright. All rights reserved. |
| Databáze: | OpenAIRE |
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