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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the mitochondrial tryparedoxin peroxidase from Leishmania braziliensis
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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the mitochondrial tryparedoxin peroxidase from Leishmania braziliensis

机译:巴西利什曼原虫线粒体类胰蛋白酶过氧化物酶的克隆,表达,纯化,结晶和初步X射线衍射分析

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摘要

Tryparedoxin peroxidase (TXNPx) is an essential constituent of the main enzymatic scavenger system for reactive oxygen species (ROS) in trypanosomatids. Genetic studies have demonstrated the importance of this system for the development and virulence of these parasites, representing a potential target for the discovery of new trypanocidal drugs. In this work, the mitochondrial TXNPx from Leishmania braziliensis was cloned, overexpressed, purified and crystallized. The crystals diffracted to 3.3 angstrom resolution and belonged to space group P4(2)2(1)2, with unit-cell parameters a = b = 131.8, c = 44.4 angstrom. These studies will contribute to a better understanding of the molecular mechanisms involved in ROS detoxification by trypanosomatids.
机译:Tryparedoxin过氧化物酶(TXNPx)是锥虫病中活性氧(ROS)的主要酶清除剂系统的重要组成部分。遗传研究表明,该系统对于这些寄生虫的发育和毒力的重要性,是发现新的锥虫病药物的潜在目标。在这项工作中,来自巴西利什曼原虫的线粒体TXNPx被克隆,过表达,纯化和结晶。晶体衍射到3.3埃分辨率,并属于空间群P4(2)2(1)2,单位晶胞参数a = b = 131.8,c = 44.4埃。这些研究将有助于更好地了解锥虫的ROS解毒所涉及的分子机制。

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