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Crystallization and preliminary structural characterization of the two actin isoforms of the malaria parasite

机译:疟原虫的两种肌动蛋白同工型的结晶和初步结构表征

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摘要

Malaria is a devastating disease caused by apicomplexan parasites of the genus Plasmodium that use a divergent actin-powered molecular motor for motility and invasion. Plasmodium actin differs from canonical actins in sequence, structure and function. Here, the purification, crystallization and secondary-structure analysis of the two Plasmodium actin isoforms are presented. The recombinant parasite actins were folded and could be purified to homogeneity. Plasmodium actins I and II were crystallized in complex with the gelsolin G1 domain; the crystals diffracted to resolutions of 1.19 and 2.2 Å and belonged to space groups P212121 and P21, respectively, each with one complex in the asymmetric unit.
机译:疟疾是由疟原虫属的apicomplexan寄生虫引起的毁灭性疾病,该寄生虫使用发散的肌动蛋白驱动的分子运动来促进运动和侵袭。疟原虫肌动蛋白在序列,结构和功能上不同于经典肌动蛋白。在这里,提出了两种疟原虫肌动蛋白同工型的纯化,结晶和二级结构分析。重组寄生虫肌动蛋白被折叠并且可以被纯化至同质。疟原虫肌动蛋白I和II与凝溶胶蛋白G1结构域复合结晶;晶体衍射至1.19和2.2Å的分辨率,分别属于空间群P212121和P21,每个空间群在不对称单元中具有一个复合物。

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