The crystal structure of D-ribulose 5-phosphate 3-epimerase (RPE) from the cyanobacterium Synechocystis was determined by X-ray crystallography to 1.6 Å resolution. The enzyme, which catalyzes the epimerization of D-ribulose 5-phosphate and D-xylulose 5-phosphate, assembles as a hexamer of (β/α)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.
|Original language||English (US)|
|Number of pages||4|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|State||Published - Sep 2004|
ASJC Scopus subject areas
- Structural Biology