Structural Studies of ROK Fructokinase YdhR from Bacillus subtilis: Insights into Substrate Binding and Fructose Specificity
| Autor: | Hui Li, Robert Jedrzejczak, Andrzej Joachimiak, Boguslaw Nocek, Marianne E. Cuff, A.J. Stein, L. Volkart |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Molecular Sequence Data
Fructose Bacillus subtilis Biology Crystallography X-Ray Fructokinase Article Substrate Specificity Fructokinases chemistry.chemical_compound Bacterial Proteins Structural Biology Transferase Amino Acid Sequence Molecular Biology rho-Associated Kinases Kinase PEP group translocation biology.organism_classification Biochemistry chemistry Phosphorylation Phosphoenolpyruvate carboxykinase Protein Binding |
| Zdroj: | Journal of Molecular Biology. 406:325-342 |
| ISSN: | 0022-2836 |
| DOI: | 10.1016/j.jmb.2010.12.021 |
| Popis: | The main pathway of bacterial sugar phosphorylation utilizes specific phosphoenolpyruvate phosphotransferase system (PTS) enzymes. In addition to the classic PTS system, a PTS-independent secondary system has been described in which nucleotide-dependent sugar kinases are used for monosaccharide phosphorylation. Fructokinase (FK), which phosphorylates d-fructose with ATP as a cofactor, has been shown to be a member of this secondary system. Bioinformatic analysis has shown that FK is a member of the "ROK" (bacterial Repressors, uncharacterized Open reading frames, and sugar Kinases) sequence family. In this study, we report the crystal structures of ROK FK from Bacillus subtilis (YdhR) (a) apo and in the presence of (b) ADP and (c) ADP/d-fructose. All structures show that YdhR is a homodimer with a monomer composed of two similar α/β domains forming a large cleft between domains that bind ADP and D-fructose. Enzymatic activity assays support YdhR function as an ATP-dependent fructose kinase. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect