Expression, purification, crystallization, and preliminary X-Ray analysis of the human UDP-glucose dehydrogenase.
UDP-glucose dehydrogenase (UGDH) catalyzes the synthesis of UDP-glucuronic acid from UDP-glucose resulting in the formation of proteoglycans that are involved in promoting normal cellular growth and migration. Overproduction of proteoglycans has been implicated in the progression of certain epithelial cancers. Here, human UGDH (hUGDH) was purified and crystallized from a solution of 0.2 M ammonium sulfate, 0.1 M Na cacodylate, pH 6.5, and 21% PEG 8000. Diffraction data were collected to a resolution of 2.8 A. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1) with unit-cell parameters a = 173.25, b = 191.16, c = 225.94 A, and alpha = beta = gamma = 90.0 degrees. Based on preliminary analysis of the diffraction data, we propose that the biological unit of hUGDH is a tetramer.
Huh
Jae Wan
JW
Department of Biochemistry and Molecular Biology, University of Ulsan College of Medicine, Seoul 138-736, South Korea.
Robinson
Robert Charles
RC
Lee
Han Sam
HS
Lee
Jae Il
JI
Heo
Yong Seok
YS
Kim
Hyun Tae
HT
Lee
Hyun Ju
HJ
Cho
Sung Woo
SW
Choe
Han
H
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D006801:Humans; D014532:Uridine Diphosphate Glucose / Q000378:metabolism; D014533:Uridine Diphosphate Glucose Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism
D014533:Uridine Diphosphate Glucose Dehydrogenase; D014532:Uridine Diphosphate Glucose