1H1Y
The structure of the cytosolic D-ribulose-5-phosphate 3-epimerase from rice complexed with sulfate
Summary for 1H1Y
| Entry DOI | 10.2210/pdb1h1y/pdb |
| Related | 1H1Z |
| Descriptor | D-RIBULOSE-5-PHOSPHATE 3-EPIMERASE, SULFATE ION (3 entities in total) |
| Functional Keywords | 3-epimerase, oxidative pentose phosphate pathway, isomerase |
| Biological source | ORYZA SATIVA (RICE) |
| Total number of polymer chains | 2 |
| Total formula weight | 48826.06 |
| Authors | Jelakovic, S.,Schulz, G.E. (deposition date: 2002-07-25, release date: 2003-01-30, Last modification date: 2024-05-08) |
| Primary citation | Jelakovic, S.,Kopriva, S.,Suss, K.,Schulz, G.E. Structure and Catalytic Mechanism of the Cytosolic D-Ribulose-5-Phosphate 3-Epimerase from Rice J.Mol.Biol., 326:127-, 2003 Cited by PubMed Abstract: Cytosolic D-ribulose-5-phosphate 3-epimerase from rice was crystallized after EDTA treatment and structurally elucidated by X-ray diffraction to 1.9A resolution. A prominent Zn(2+) site at the active center was established in a soaking experiment. The structure was compared with that of the EDTA-treated crystalline enzyme from the chloroplasts of potato plant leaves showing some structural differences, in particular the "closed" state of a strongly conserved mobile loop covering the substrate at its putative binding site. The previous proposal for the active center was confirmed and the most likely substrate binding position and conformation was derived from the locations of the bound zinc and sulfate ions and of three water molecules. Assuming that the bound zinc ion is an integral part of the enzyme, a reaction mechanism involving a well-stabilized cis-enediolate intermediate is suggested. PubMed: 12547196DOI: 10.1016/S0022-2836(02)01374-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.87 Å) |
Structure validation
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