人喹啉酸磷酸核糖基转移酶的结晶及初步X射线晶体学分析
Crystallization and preliminary X-ray crystallographic analysis of human quinolinate phosphoribosyltransferase.
作者信息
Kang Gil Bu, Kim Mun-Kyoung, Youn Hyung-Seop, An Jun Yop, Lee Jung-Gyu, Park Kyoung Ryoung, Lee Sung Hang, Kim Yongseong, Fukuoka Shin-Ichi, Eom Soo Hyun
机构信息
School of Life Sciences, Gwangju Institute of Science and Technology, Gwangju 500-712, Republic of Korea.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):38-40. doi: 10.1107/S1744309110041011. Epub 2010 Dec 21.
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 Å resolution. Native Hs-QPRTase crystals belonged to space group P2(1), with unit-cell parameters a=76.2, b=137.1, c=92.7 Å, β=103.8°. Assuming the presence of six molecules in the asymmetric unit, the calculated Matthews coefficient is 2.46 Å3 Da(-1), which corresponds to a solvent content of 49.9%.
喹啉酸磷酸核糖基转移酶（QPRTase）是一种关键的烟酰胺腺嘌呤二核苷酸（NAD）生物合成酶，它催化喹啉酸向5-磷酸核糖-1-焦磷酸的转移，生成烟酸单核苷酸。人类QPRTase（Hs-QPRTase）在纯化过程中呈现为六聚体，并对该蛋白质进行了结晶。收集了衍射数据并在2.8 Å分辨率下进行了处理。天然Hs-QPRTase晶体属于空间群P2(1)，晶胞参数为a = 76.2、b = 137.1、c = 92.7 Å，β = 103.8°。假设不对称单位中存在六个分子，计算得到的马修斯系数为2.46 ų Da⁻¹，这对应于49.9%的溶剂含量。
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