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

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

Volume: 13 Issue: 8

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 and Han Choe

Affiliation:

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

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.

Cite this article as:

Wan Huh Jae, Charles Robinson Robert, Sam Lee Han, Il Lee Jae, Seok Heo Yong, Tae Kim Hyun, Ju Lee Hyun, Woo Cho Sung and Choe Han, Expression, Purification, Crystallization, and Preliminary X-Ray Analysis of the Human UDP-Glucose Dehydrogenase, Protein & Peptide Letters 2006; 13 (8) . https://dx.doi.org/10.2174/092986606777841253

DOI https://dx.doi.org/10.2174/092986606777841253	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305