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

doi:10.2174/092986606777841253

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 journal › Article › peer-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 language	English
Pages (from-to)	859-862
Number of pages	4
Journal	Protein and Peptide Letters
Volume	13
Issue number	8
DOIs	https://doi.org/10.2174/092986606777841253
Publication status	Published - 2006
Externally published	Yes

Keywords

Crystallization
GMDH
UDP-glucose
UDP-glucuronic acid
UGDH

ASJC Scopus subject areas

Structural Biology
Biochemistry

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.2174/092986606777841253

Cite this

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title = "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 {\AA}. 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 {\AA}, 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 = "Crystallization, GMDH, UDP-glucose, UDP-glucuronic acid, UGDH",

author = "Jae, {Wan Huh} and Robinson, {Robert Charles} and Han, {Sam Lee} and Jae, {Il Lee} and Yong, {Seok Heo} and Hyun, {Tae Kim} and Hyun, {Ju Lee} and Sung, {Woo Cho} and Han Choe",

year = "2006",

doi = "10.2174/092986606777841253",

language = "English",

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pages = "859--862",

journal = "Protein and Peptide Letters",

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T1 - Expression, purification, crystallization, and preliminary X-ray analysis of the human UDP-glucose dehydrogenase

AU - Jae, Wan Huh

AU - Robinson, Robert Charles

AU - Han, Sam Lee

AU - Jae, Il Lee

AU - Yong, Seok Heo

AU - Hyun, Tae Kim

AU - Hyun, Ju Lee

AU - Sung, Woo Cho

AU - Choe, Han

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

KW - Crystallization

KW - GMDH

KW - UDP-glucose

KW - UDP-glucuronic acid

KW - UGDH

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SP - 859

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JO - Protein and Peptide Letters

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ER -

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

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

Access to Document

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