Expression, purification, crystallization, and preliminary X-ray analysis of the human UDP-glucose dehydrogenase

Wan Huh Jae, Robert Charles Robinson, Sam Lee Han, Il Lee Jae, Seok Heo Yong, Tae Kim Hyun, Ju Lee Hyun, Woo Cho Sung, Han Choe

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)

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 P2 12 12 1 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.

Original languageEnglish
Pages (from-to)859-862
Number of pages4
JournalProtein and Peptide Letters
Volume13
Issue number8
DOIs
Publication statusPublished - 2006

Keywords

  • Crystallization
  • GMDH
  • UDP-glucose
  • UDP-glucuronic acid
  • UGDH

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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