Crystallization and preliminary X-ray crystallographic study of UDP-glucose pyrophosphorylase (UGPase) from Helicobacter pylori.
UDP-glucose pyrophosphorylase (UGPase) catalyzes the synthesis of UDP-glucose, an essential metabolite in all living organisms. An X-ray crystallographic study of UGPase from Helicobacter pylori has been performed in order to elucidate its role in the regulation of this important metabolic pathway. UGPase was crystallized from 0.1 M sodium acetate trihydrate pH 4.6, 2.0 M ammonium sulfate and 0.1 M guanidine-HCl. According to diffraction data collected at a resolution of 2.9 A using a synchrotron-radiation source, the crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 91.47, b = 98.61, c = 245.70 A, alpha = beta = gamma = 90.0 degrees.
Kim
Hun
H
Department of Molecular Cell Biology, Center for Molecular Medicine, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, South Korea.
Wu
Chun Ai
CA
Kim
Dong Young
DY
Han
Young-Hyun
YH
Ha
Sung Chul
SC
Kim
Chun-Sang
CS
Suh
Se Won
SW
Kim
Kyeong Kyu
KK
D003460:Crystallization; D018360:Crystallography, X-Ray; D016480:Helicobacter pylori / Q000201:enzymology*; D005957:UTP-Glucose-1-Phosphate Uridylyltransferase / Q000737:chemistry*
D005957:UTP-Glucose-1-Phosphate Uridylyltransferase