Structural analysis of CPF_2247, a novel α-amylase from Clostridium perfringens
| Autor: | Christopher P. Stuart, Elizabeth Ficko-Blean, Alisdair B. Boraston |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences biology Glycogen 030302 biochemistry & molecular biology Clostridium perfringens medicine.disease_cause Biochemistry Sequence identity 03 medical and health sciences chemistry.chemical_compound Enzyme chemistry Structural Biology Amylose Hydrolase medicine biology.protein Glycoside hydrolase Amylase Molecular Biology 030304 developmental biology |
| Zdroj: | Proteins: Structure, Function, and Bioinformatics. 79:2771-2777 |
| ISSN: | 0887-3585 |
| DOI: | 10.1002/prot.23116 |
| Popis: | CPF_2247 from Clostridium perfringens ATCC 13124 was identified as a putative carbohydrate-active enzyme by its low sequence identity to endo-β-1,4-glucanases belonging to family 8 of the glycoside hydrolase classification. The X-ray crystal structure of CPF_2247 determined to 2.0 A resolution by single-wavelength anomalous dispersion using seleno-methionine-substituted protein revealed an (α/α)6 barrel fold. A large cleft on the surface of the protein contains residues that are structurally conserved with key elements of the catalytic machinery in clan GH-M glycoside hydrolases. Assessment of CPF_2247 as a carbohydrate-active enzyme disclosed α-glucanase activity on amylose, glycogen, and malto-oligosaccharides. Proteins 2011;. © 2011 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
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