Structure determination and analysis of a bacterial chymotrypsin fromCellulomonas bogoriensis
| Autor: | Marc Kolkman, Brian E. Jones, Andrew Shaw, R. Bott, M. L. Saldajeno |
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| Rok vydání: | 2007 |
| Předmět: |
Protein Folding
Protein Conformation Stereochemistry Molecular Sequence Data Biophysics Crystal structure Biochemistry Substrate Specificity Bacterial Proteins X-Ray Diffraction Structural Biology Hydrolase Genetics Chymotrypsin Protein Structure Communications Alkaliphile Amino Acid Sequence Cellulomonas chemistry.chemical_classification Sequence Homology Amino Acid biology Chemistry Hydrogen bond Hydrogen Bonding Condensed Matter Physics Crystallography Enzyme Cellulomonas bogoriensis biology.protein Crystallization |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63:266-269 |
| ISSN: | 1744-3091 |
| Popis: | The crystal structure of a secreted chymotrypsin from the alkaliphile Cellulomonas bogoriensis has been determined using data to 1.78 A resolution and refined to a crystallographic R factor of 0.167. The crystal structure reveals a large P1 substrate-specificity pocket, as expected for chymotrypsins. The structure is compared with close structural homologues. This comparison does not reveal clear reasons for the alkali tolerance of the enzyme, but the greater compactness of the structure and lowered hydrogen bonding may play a role. |
| Databáze: | OpenAIRE |
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