Crystallization and preliminary X-ray crystallographic analysis of human quinolinate phosphoribosyltransferase

被引：3

作者：

Kang, Gil Bu ^{[1
]}

Kim, Mun-Kyoung ^{[1
]}

Youn, Hyung-Seop ^{[1
]}

An, Jun Yop ^{[1
]}

Lee, Jung-Gyu ^{[1
]}

Park, Kyoung Ryoung ^{[1
]}

Lee, Sung Hang ^{[2
]}

Kim, Yongseong ^{[3
]}

Fukuoka, Shin-Ichi ^{[4
]}

Eom, Soo Hyun ^{[1
]}

机构：

[1] Gwangju Inst Sci & Technol, Sch Life Sci, Kwangju 500712, South Korea

[2] Chosun Univ, Sch Med, Res Ctr Resistant Cells, Kwangju, South Korea

[3] Kyungnam Univ, Dept Chem, Masan 631701, South Korea

[4] Aoyama Gakuin Univ, Coll Sci & Engn, Dept Chem & Biol Sci, Mol Cell Biol Lab, Kanagawa 2298558, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷

关键词：

ACID PHOSPHORIBOSYLTRANSFERASE; CRYSTAL-STRUCTURE; HUNTINGTONS-DISEASE; BRAIN; PURIFICATION; LIVER;

D O I：

10.1107/S1744309110041011

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Quinolinate phosphoribosyltransferase (QPRTase) is a key NAD-biosynthetic enzyme which catalyzes the transfer of quinolinic acid to 5-phosphoribosyl-1-pyrophosphate, yielding nicotinic acid mononucleotide. Homo sapiens QPRTase (Hs-QPRTase) appeared as a hexamer during purification and the protein was crystallized. Diffraction data were collected and processed at 2.8 angstrom resolution. Native Hs-QPRTase crystals belonged to space group P2(1), with unit-cell parameters a = 76.2, b = 137.1, c = 92.7 angstrom, beta = 103.8 degrees. Assuming the presence of six molecules in the asymmetric unit, the calculated Matthews coefficient is 2.46 angstrom(3) Da(-1), which corresponds to a solvent content of 49.9%.

引用

页码：38 / 40

页数：3

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