Summary for 3OHR
| Entry DOI | 10.2210/pdb3ohr/pdb |
| Related | 1XC3 3LM9 |
| Descriptor | Putative fructokinase, ADENOSINE-5'-DIPHOSPHATE, ZINC ION, ... (5 entities in total) |
| Functional Keywords | metal dependent, adp binding, d-fructose binding, structural genomics, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, rok family, fructokinase, reductive methylation, transferase |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 1 |
| Total formula weight | 34020.88 |
| Authors | Nocek, B.,Volkart, L.,Cuff, M.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2010-08-17, release date: 2010-09-15, Last modification date: 2025-03-26) |
| Primary citation | Nocek, B.,Stein, A.J.,Jedrzejczak, R.,Cuff, M.E.,Li, H.,Volkart, L.,Joachimiak, A. Structural studies of ROK fructokinase YdhR from Bacillus subtilis: insights into substrate binding and fructose specificity. J.Mol.Biol., 406:325-342, 2011 Cited by PubMed Abstract: 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. PubMed: 21185308DOI: 10.1016/j.jmb.2010.12.021 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.66 Å) |
Structure validation
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