The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an α/β hydrolase fold
| Autor: | T. Haag, Harald Sobek, H.-J. Hecht, K.-H. Van Pee, O. Pfeifer |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular Hydrolases Protein Conformation Stereochemistry Molecular Sequence Data Streptomyces aureofaciens Crystallography X-Ray Biochemistry Catalysis Cofactor Bacterial Proteins Structural Biology Oxidoreductase Haloperoxidase Hydrolase Catalytic triad Genetics Amino Acid Sequence Bromoperoxidase chemistry.chemical_classification Binding Sites Sequence Homology Amino Acid biology biology.organism_classification Enzyme Peroxidases chemistry biology.protein Sequence Alignment |
| Zdroj: | Nature Structural Biology. 1:532-537 |
| ISSN: | 1072-8368 |
| DOI: | 10.1038/nsb0894-532 |
| Popis: | The crystal structure of the bromoperoxidase A2 from Streptomyces aureofaciens (ATCC 10762) has been determined by isomorphous replacement and refined to 2.05 A resolution with an R-value of 18.4%. The enzyme catalyzes the bromination of organic compounds in the presence of bromide and peroxide. The structure confirms the absence of cofactors such as metal ions or haem groups and shows the general topology of the alpha/beta hydrolase fold. The active centre is at the end of a deep pocket and includes a catalytic triad of Ser 98, Asp 228 and His 257. The active centre is connected by a narrow tunnel to a second pocket on the enzyme surface. |
| Databáze: | OpenAIRE |
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