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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum.
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Structure of glyceraldehyde-3-phosphate dehydrogenase from Plasmodium falciparum.

机译：glyceraldehyde-3-phosphate结构脱氢酶从恶性疟原虫。

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摘要

The malaria parasite Plasmodium falciparum is responsible for about two million deaths annually, making it important to obtain information about enzymes from this organism that represent potential drug targets. The gene for P. falciparum glyceraldehyde-3-phosphate dehydrogenase (PfGAPDH) has been cloned and the protein expressed as a hexahistidine-tagged recombinant protein in Escherichia coli. The recombinant protein has been crystallized and its three-dimensional structure determined. One molecule of the cofactor NAD(+) is bound to each of the four subunits in the tetrameric enzyme. The major structural feature distinguishing human GAPDH from PfGAPDH is the insertion of a dipeptide (-KG-) in the so-called S loop. This insert, together with other characteristic single-amino-acid substitutions, alters the chemical environment of the groove that encompasses the R dyad and that links adjacent cofactor-binding sites and may be responsible for the selective inhibition of the enzyme by ferriprotoporphyrin IX.
机译：恶性疟原虫负责约二百万人死亡每年,获得很重要酶的生物信息代表潜在的药物靶点。恶性疟原虫glyceraldehyde-3-phosphate脱氢酶(PfGAPDH)已经被克隆的作为一个hexahistidine-tagged蛋白表达重组蛋白在大肠杆菌。重组蛋白结晶及其三维结构确定。分子代数余子式的NAD(+)绑定四聚物的四个亚基的酶。的主要结构特征区分人类从PfGAPDH GAPDH是插入二肽(公斤)所谓的循环。插入,连同其他的特点个氨基酸替换,改变了化学环境的槽包含的R二分体和相邻的链接cofactor-binding网站和负责酶的选择性抑制作用ferriprotoporphyrin IX .

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