Structure of D-ribulose 5-phosphate 3-epimerase from Synechocystis to 1.6 A resolution.
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.
Wise
Eric L
EL
Deparment of Biochemistry, University of Wisconsin, Madison, WI 53706, USA.
Akana
Julie
J
Gerlt
John A
JA
Rayment
Ivan
I
D001665:Binding Sites; D002238:Carbohydrate Epimerases / Q000737:chemistry* / Q000235:genetics; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D003600:Cytosol / Q000201:enzymology; D008958:Models, Molecular; D020133:Reverse Transcriptase Polymerase Chain Reaction; D046939:Synechocystis / Q000201:enzymology* / Q000235:genetics
D002238:Carbohydrate Epimerases; C022553:ribulosephosphate 3-epimerase