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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Expression, purification and crystallization of the Plasmodium falciparum enoyl reductase.
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Expression, purification and crystallization of the Plasmodium falciparum enoyl reductase.

机译：的表达、纯化和结晶恶性疟原虫enoyl还原酶。

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摘要

New hope has been gained in the control of the malaria parasite Plasmodium falciparum (pf) with the discovery that the parasite contains a prokaryotic type II fatty-acid synthase (FAS). Since enzymes of this type are absent in humans, they are potential targets for the development of new drugs. The enoyl reductase enzyme (ENR) belonging to this pathway is of particular interest because it has been shown to be inhibited by submicromolar concentrations of the antimicrobial agent triclosan. Here, the development of an efficient overexpression system for pfENR as a fusion protein with maltose-binding protein, its simple one-step purification and cleavage from its fusion protein and crystallization under new conditions with bound NAD(+) cofactor and triclosan are reported. The crystals belong to the space group P2(1), with approximate unit-cell parameters a = 88.2, b = 82.4, c = 94.8 A, beta = 90.77 degrees, and contain a tetramer in the asymmetric unit. Cryocooled crystals (100 K) diffracted to beyond 2.2 A resolution at the Daresbury Synchrotron Radiation Source.
机译：新的希望已经得到控制的恶性疟原虫(pf)发现这种寄生虫包含一个原核的II型脂肪酸合酶(FAS)。因为这种类型的酶在人类中缺席,他们发展的潜在目标新药。属于这个途径是特殊的因为它已被证明是感兴趣submicromolar浓度抑制的抗菌剂三氯生。一个有效的超表达系统的发展pfENR作为融合蛋白maltose-binding蛋白质,其简单的一步融合蛋白的净化和乳沟在新的条件下,结晶绑定NAD(+)代数余子式和三氯生。水晶属于空间群P2 (1),近似的晶胞参数= 88.2,b= 82.4, c = 94.8,β= 90.77度,包含一个四聚物的不对称单元。Cryocooled晶体衍射(100 K)2.2在位于达斯伯里同步解决辐射源。

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