Acta Crystallographica Section D 2004-09-01

Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution.

Eric L Wise, Julie Akana, John A Gerlt, Ivan Rayment

文献索引：Acta Crystallogr. D Biol. Crystallogr. 60(Pt 9) , 1687-90, (2004)

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摘要

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.