Crystal structure of pyrimidine-nucleoside phosphorylase fromBacillus subtilisin complex with imidazole and sulfate
| Autor: | A.G. Gabdoulkhakov, Ch. Betzel, A. A. Lashkov, I.I. Prokofev, V.V. Balaev |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein Conformation Stereochemistry Biophysics Pyrimidine-nucleoside phosphorylase Bacillus subtilis Crystallography X-Ray Cleavage (embryo) Biochemistry Substrate Specificity Research Communications 03 medical and health sciences chemistry.chemical_compound Glycogen phosphorylase 0302 clinical medicine Structural Biology Catalytic Domain Genetics Transferase Imidazole Amino Acid Sequence Binding Sites biology Sulfates Imidazoles Pyrimidine Phosphorylases Condensed Matter Physics biology.organism_classification Uridine 030104 developmental biology chemistry 030220 oncology & carcinogenesis Crystallization Thymidine |
| Zdroj: | Acta Crystallographica Section F Structural Biology Communications. 74:193-197 |
| ISSN: | 2053-230X |
| Popis: | Pyrimidine-nucleoside phosphorylase catalyzes the phosphorolytic cleavage of thymidine and uridine with equal activity. Investigation of this protein is essential for anticancer drug design. Here, the structure of this protein fromBacillus subtilisin complex with imidazole and sulfate is reported at 1.9 Å resolution, which is an improvement on the previously reported structure at 2.6 Å resolution. The localization and position of imidazole in the nucleoside-binding site reflects the possible binding of ligands that possess an imidazole ring. |
| Databáze: | OpenAIRE |
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