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 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) |
|---|---|
| Pages (from-to) | 1687-1690 |
| Number of pages | 4 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 60 |
| Issue number | 9 |
| DOIs | |
| State | Published - Sep 2004 |
ASJC Scopus subject areas
- Structural Biology