Crystallization and preliminary X-ray crystallographic analysis of orotate phosphoribosyltransferase from Helicobacter pylori.
Orotic acid phosphoribosyltransferase (PyrE) (EC 2.4.2.10) is a key enzyme in de novo uridine monophosphate (UMP) biosynthesis. It catalyzes the reaction between orotic acid and 5-phosphoribosyl-1-pyrophosphate (PRPP) to yield orotidine monophosphate (OMP), which is transformed to uridine monophosphate by decarboxylation. H. pylori PyrE was crystallized at 294 +/- 1 K by the hanging drop vapor-diffusion method. The crystals belong to the space group P2(1)2(1)2(1) with unit-cell dimensions a = 95.8, b = 104.9, c = 281.1 A, alpha = beta = gamma = 90 degrees. A set of diffraction data was collected to 3.29 A resolution using synchrotron X-ray radiation.
Kim
Mun-Kyoung
MK
Department of Life Science, Kwangju Institute of Science and Technology, Gwangju 500-712, Korea.
Song
Hye-Eun
HE
Kim
Yun Sik
YS
Rho
Seong-Hwan
SH
Im
Young Jun
YJ
Lee
Jun Hyuck
JH
Kang
Gil Bu
GB
Eom
Soo Hyun
SH
D003460:Crystallization / Q000379:methods*; D018360:Crystallography, X-Ray / Q000379:methods*; D004926:Escherichia coli / Q000235:genetics; D016480:Helicobacter pylori / Q000201:enzymology*; D009962:Orotate Phosphoribosyltransferase / Q000737:chemistry*; D011487:Protein Conformation; D012486:Salmonella typhimurium / Q000235:genetics; D016415:Sequence Alignment; D014162:Transfection
D009962:Orotate Phosphoribosyltransferase