A structural snapshot of the multiple working states of the Mpox virus helicase-primase D5.

Yingying Guo, Renhong Yan
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Abstract

The Mpox virus (or Monkeypox virus, MPXV) uses its own encoded proteins to form a replication machine that replicates the viral genome in the host cell cytoplasm, making this machinery a key target for antiviral drug design. The D5 (also known as the OPG117 or E5) protein, a bi-functional helicase-primase enzyme, is crucial in the MPXV replication machinery and genome uncoating process. Recently, cryo-electron microscopy (cryo-EM) structures of D5 in multiple states have been determined. These structures have elucidated the full trajectory of the MPXV D5 helicase-primase as it moves along single-stranded DNA, providing unprecedented advancements in the molecular dynamics and unwinding mechanism. This structural snapshot describes the structural features of the D5 protein and dissects the broader implications of its pivotal role in MPXV replication.

Mpox 病毒螺旋酶-primase D5 多种工作状态的结构快照。
痘病毒(或称猴痘病毒,MPXV)利用自身编码的蛋白质组成复制机器,在宿主细胞胞质中复制病毒基因组,因此这一机器成为抗病毒药物设计的关键靶点。D5(又称 OPG117 或 E5)蛋白是一种双功能螺旋酶-primase 酶,在 MPXV 复制机器和基因组解衣过程中至关重要。最近,人们确定了 D5 在多种状态下的低温电子显微镜(cryo-EM)结构。这些结构阐明了 MPXV D5 螺旋酶-原基酶沿单链 DNA 运动的全部轨迹,为分子动力学和解旋机制提供了前所未有的进展。本结构快照描述了 D5 蛋白的结构特征,并剖析了它在 MPXV 复制中的关键作用所产生的广泛影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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