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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >The 2C putative helicase of echovirus 30 adopts a hexameric ring-shaped structure.
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The 2C putative helicase of echovirus 30 adopts a hexameric ring-shaped structure.

机译：2摄氏度的解旋酶艾柯病毒30实行hexameric环形结构。

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摘要

The 2C protein, which is an essential ATPase and one of the most conserved proteins across the Picornaviridae family, is an emerging antiviral target for which structural and functional characterization remain elusive. Based on a distant relationship to helicases of small DNA viruses, piconavirus 2C proteins have been predicted to unwind double-stranded RNAs. Here, a terminally extended variant of the 2C protein from echovirus 30 has been studied by means of enzymatic activity assays, transmission electron microscopy, atomic force microscopy and dynamic light scattering. The transmission electron-microscopy technique showed the existence of ring-shaped particles with approximately 12 nm external diameter. Image analysis revealed that these particles were hexameric and resembled those formed by superfamily 3 DNA virus helicases.
机译：2 c蛋白,这是一个基本的atp酶和在最保守的蛋白质引起家庭,是一个新兴的抗病毒药物结构和功能的目标描述仍然是难以捉摸的。遥远的小DNA解旋酶的关系病毒、微小核糖核酸病毒2 c蛋白预测放松双链rna。晚期的扩展变体2 c蛋白从艾柯病毒30研究通过酶活性测定,透射电子显微镜、原子力显微镜和动态光散射。电子显微镜技术显示,环形粒子的存在外部直径约12海里。分析显示,这些粒子hexameric和类似这些形成的总科3病毒DNA解旋酶。

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