1TQJ

Crystal structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 angstrom resolution

1TQJ の概要

• エントリーDOI: 10.2210/pdb1tqj/pdb
• 分子名称: Ribulose-phosphate 3-epimerase (2 entities in total)
• 機能のキーワード: beta-alpha barrel epimerase, isomerase
• 由来する生物種: Synechocystis sp.
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 149986.82

構造登録者

Wise, E.L.,Akana, J.,Gerlt, J.A.,Rayment, I. (登録日: 2004-06-17, 公開日: 2004-08-31, 最終更新日: 2024-02-14)

主引用文献

Wise, E.L.,Akana, J.,Gerlt, J.A.,Rayment, I.
Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution.
Acta Crystallogr.,Sect.D, 60:1687-1690, 2004

PubMed Abstract: The crystal structure of D-ribulose 5-phosphate 3-epimerase (RPE) from the cyanobacterium Synechocystis was determined by X-ray crystallography to 1.6 A resolution. The enzyme, which catalyzes the epimerization of D-ribulose 5-phosphate and D-xylulose 5-phosphate, assembles as a hexamer of (beta/alpha)(8)-barrels in the crystallographic asymmetric unit. The active site is highly similar to those of two previously reported RPEs and provides further evidence for essential catalytic roles for several active-site residues.

PubMed: 15333955
DOI: 10.1107/S0907444904015896

実験手法

X-RAY DIFFRACTION (1.6 Å)