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
收藏
页码：38 / 40
页数：3
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