Among the malaria-causing parasites, the deadliest is Plasmodium falciparum, which accounts for the majority of the fatalities. As the infection progresses inside erythrocytes, major cellular and metabolic changes take place. For its own growth, the parasite relies on the accumulation of phospholipids, which are essential for membrane synthesis. Within the Kennedy pathway, the P. falciparum choline kinase (PfChoK) has a central role in the biosynthesis of phosphatidylcholine and its selective inhibition leads to the parasite arrest and eradication. Here, we report the crystal structure of the apo and the ADP-bound form of choline kinase from Plasmodium falciparum at 2.0 and 2.2 Å resolution, respectively. These new structural data will facilitate the implementation of effective structure-based drug development strategies against PfChoK in the fight against malaria.

中文翻译：

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恶性疟原虫的Apo晶体结构和胆碱激酶的ADP结合形式

在引起疟疾的寄生虫中，致死率最高的是恶性疟原虫，占死亡人数的绝大部分。随着感染在红细胞内部进行，主要的细胞和代谢发生变化。对于其自身的生长，该寄生虫依赖于磷脂的积累，这对于膜合成是必不可少的。在肯尼迪途径中，恶性疟原虫胆碱激酶（PfChoK）在磷脂酰胆碱的生物合成中起着核心作用，其选择性抑制导致寄生虫的停滞和根除。在这里，我们报告恶性疟原虫的载脂蛋白的晶体结构和胆碱激酶的ADP结合形式分别在2.0和2.2Å分辨率下。这些新的结构数据将有助于在抗击疟疾中实施针对PfChoK的有效的基于结构的药物开发策略。