Structural highlights
Function
[RPE_SYNY3] Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution.,Wise EL, Akana J, Gerlt JA, Rayment I Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1687-90. Epub 2004, Aug 26. PMID:15333955[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wise EL, Akana J, Gerlt JA, Rayment I. Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution. Acta Crystallogr D Biol Crystallogr. 2004 Sep;60(Pt 9):1687-90. Epub 2004, Aug 26. PMID:15333955 doi:http://dx.doi.org/10.1107/S0907444904015896
