The Rice Yellow Mottle sobemovirus (RYMV) belongs to the most damaging pathogens devastating rice fields in Africa. P1, a key protein for RYMV, was reported as a potent RNAi suppressor counteracting RNA silencing in plant reporter systems. Here we describe the complete 3D structure and dynamics of P1. Its N-terminal region contains ZnF1, a structural CCCC-type zinc finger strongly affine to zinc and a prominent short helix, rendering this region poorly amenable to structural changes. P1 C-terminal region contains ZnF2, an atypical HCHC-type ZnF that does not belong to any existing class of Zn finger proteins. ZnF2 appeared much less affine to zinc and more sensitive to oxidizing environments than ZnF1, and may serve as a sensor of plant redox status. The structure helped us to identify key residues essential for RYMV infectivity and spread in rice tissues through their participation in P1 oligomerization and folding. Altogether, our results provide the first complete structure of an antiviral silencing suppressor encoded by a virus infecting rice and highlight P1 structural and dynamical properties that may serve RYMV functions to infect and invade its host plant.

中文翻译：

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原始结构折叠是多任务P1的基础，P1是水稻黄斑驳病毒编码的沉默抑制因子

稻黄斑疹病毒（RYMV）是破坏非洲稻田的最具破坏性的病原体。据报道，P1是RYMV的关键蛋白，是一种有效的RNAi抑制剂，可抵消植物报告系统中的RNA沉默。在这里，我们描述了P1的完整3D结构和动力学。它的N端区域包含ZnF1，这是一种结构CCCC型锌指，与锌有很强的亲和力，并且具有明显的短螺旋，使该区域难以适应结构变化。P1 C端区域包含ZnF2，这是一种不属于任何现有Zn指状蛋白的非典型HCHC型ZnF。与ZnF1相比，ZnF2对锌的亲和力小得多，对氧化环境的敏感性更高，并且可以用作植物氧化还原状态的传感器。该结构帮助我们确定了RYMV感染力所必需的关键残基，并通过它们参与P1寡聚和折叠而在水稻组织中传播。总之，我们的结果提供了由感染水稻的病毒编码的抗病毒沉默抑制剂的第一个完整结构，并突出了P1的结构和动力学特性，可发挥RYMV功能来感染和侵袭其寄主植物。