Expression, Purification, Crystallization, and Preliminary X-Ray Analysis of the Human UDP-Glucose Dehydrogenase
Abstract: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 Å . The crystal belongs to the orthorhombic space group P212121 with unit-cell parameters a = 173.25, b = 191.16, c = 225.94 Å , and α = β = γ = 90.0 °. Based on preliminary analysis of the diffraction data, we propose that the biological unit of hUGDH is a tetramer.
Document Type: Research Article
Affiliations: Department of Biochemistry and Molecular Biology, cDepartment of Physiology, dResearch Institute for Biomacromolecules, University of Ulsan College of Medicine, Seoul 138-736, South Korea.
Publication date: 2006-08-01
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