Expression, Purification, Crystallization, and Preliminary X-Ray Analysis of the Human UDP-Glucose Dehydrogenase

Author(s): Jae Wan Huh, Robert Charles Robinson, Han Sam Lee, Jae Il Lee, Yong Seok Heo, Hyun Tae Kim, Hyun Ju Lee, Sung Woo Cho, Han Choe.

Journal Name: Protein & Peptide Letters

Volume 13 , Issue 8 , 2006

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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.

Keywords: UGDH, GMDH, crystallization, UDP-glucose, UDP-glucuronic acid

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Article Details

Year: 2006
Page: [859 - 862]
Pages: 4
DOI: 10.2174/092986606777841253
Price: $58

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