1H1Z

The structure of the cytosolic D-ribulose-5-phosphate 3-epimerase from rice complexed with sulfate and zinc

1H1Z の概要

• エントリーDOI: 10.2210/pdb1h1z/pdb
• 関連するPDBエントリー: 1H1Y
• 分子名称: D-RIBULOSE-5-PHOSPHATE 3-EPIMERASE, ZINC ION, SULFATE ION (3 entities in total)
• 機能のキーワード: 3-epimerase, oxidative pentose phosphate pathway, isomerase
• 由来する生物種: ORYZA SATIVA (RICE)
• 細胞内の位置: Cytoplasm: Q9SE42
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48956.87

構造登録者

Jelakovic, S.,Schulz, G.E. (登録日: 2002-07-25, 公開日: 2003-01-30, 最終更新日: 2024-05-08)

主引用文献

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

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: 12547196
DOI: 10.1016/S0022-2836(02)01374-8

実験手法

X-RAY DIFFRACTION (3.4 Å)