恶性疟原虫磷酸葡萄糖异构酶的结晶及初步X射线晶体学研究
Crystallization and preliminary X-ray crystallographic study of phosphoglucose isomerase from Plasmodium falciparum.
作者信息
Aoki Ken-ichi, Tanaka Nobutada, Kusakabe Yoshio, Fukumi Chiharu, Haga Arayo, Nakanishi Masayuki, Kitade Yukio, Nakamura Kazuo T
机构信息
School of Pharmacy, Showa University, Tokyo 142-8555, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Mar 1;66(Pt 3):333-6. doi: 10.1107/S1744309110001740. Epub 2010 Feb 25.
Abstract
Phosphoglucose isomerase (PGI) is a key enzyme in glycolysis and glycogenesis that catalyses the interconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P). For crystallographic studies, PGI from the human malaria parasite Plasmodium falciparum (PfPGI) was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data to 1.5 A resolution were collected from an orthorhombic crystal form belonging to space group P2(1)2(1)2(1) with unit-cell parameters a = 103.3, b = 104.1, c = 114.6 A. Structural analysis by molecular replacement is in progress.
摘要
磷酸葡萄糖异构酶（PGI）是糖酵解和糖原生成过程中的关键酶，催化6-磷酸葡萄糖（G6P）和6-磷酸果糖（F6P）的相互转化。为进行晶体学研究，来自人类疟原虫恶性疟原虫（PfPGI）的PGI在大肠杆菌中过量表达，采用悬滴气相扩散法进行纯化和结晶。从属于空间群P2(1)2(1)2(1)、晶胞参数a = 103.3、b = 104.1、c = 114.6 Å的正交晶型中收集到了分辨率为1.5 Å的X射线衍射数据。目前正在通过分子置换进行结构分析。
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