L-A virus at 3.4 Å resolution reveals particle architecture and mRNA decapping mechanism
L-A virus at 3.4 Å resolution reveals particle architecture and mRNA decapping mechanism
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DOI：
10.1038/nsb844
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发表时间：
2002-10-01
期刊：
影响因子：
--
通讯作者：
Johnson, JE
中科院分区：
文献类型：
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作者：
Naitow, H;Tang, JH;Johnson, JE
酵母L-A病毒的结构通过X射线晶体学在3.4埃分辨率下确定。L-A dsRNA病毒的直径为400埃，含有60个外壳蛋白不对称二聚体的单一蛋白壳，这是dsRNA病毒内部蛋白壳的共同特征，可能与其独特的转录和复制模式有关。每个二聚体中的两个相同的亚基处于非等效环境中，并且在特定的表面区域中显示出实质上不同的构象。L-A病毒使细胞mRNA脱帽以有效地翻译其自身的脱帽mRNA。我们的结构揭示了一个沟槽在活性位点的decapping反应，并建议附近的残基在反应中的作用。
The structure of the yeast L-A virus was determined by X-ray crystallography at 3.4 Angstrom resolution. The L-A dsRNA virus is 400 Angstrom in diameter and contains a single protein shell of 60 asymmetric dimers of the coat protein, a feature common among the inner protein shells of dsRNA viruses and probably related to their unique mode of transcription and replication. The two identical subunits in each dimer are in non-equivalent environments and show substantially different conformations in specific surface regions. The L-A virus decaps cellular mRNA to efficiently translate its own uncapped mRNA. Our structure reveals a trench at the active site of the decapping reaction and suggests a role for nearby residues in the reaction.