Structures of apo and complexed Escherichia coli glycinamide ribonucleotide transformylase
| Autor: | Chen-Chen Kan, Zuzana Hostomska, Cheryl A. Janson, Robert J. Almassy |
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| Rok vydání: | 1992 |
| Předmět: |
Hydroxymethyl and Formyl Transferases
Models Molecular Phosphoribosylglycinamide formyltransferase Protein Conformation Stereochemistry Beta sheet Protein structure X-Ray Diffraction Computer Graphics Escherichia coli Binding site Ternary complex Phosphoribosylglycinamide Formyltransferase chemistry.chemical_classification Binding Sites Crystallography Multidisciplinary biology Substrate (chemistry) Active site Hydrogen Bonding Recombinant Proteins Enzyme chemistry biology.protein Apoproteins Acyltransferases Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 89:6114-6118 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.89.13.6114 |
| Popis: | The three-dimensional structure of phosphoribosylglycinamide formyltransferase (10-formyltetrahydrofolate:5'-phosphoribosylglycinamide formyltransferase, EC 2.1.2.2) has been solved both as an apoenzyme at 2.8-A resolution and as a ternary complex with the substrate glycinamide ribonucleotide and a folate inhibitor at 2.5-A resolution. The structure is a modified doubly wound alpha/beta sheet with flexibility in the active site, including a disordered loop in the apo structure, which is ordered in the ternary complex structure. This enzyme is a target for anti-cancer therapy and now for structure-based drug design. |
| Databáze: | OpenAIRE |
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