Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA
Structure of foot-and-mouth disease virus RNA-dependent RNA polymerase and its complex with a template-primer RNA
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DOI：
10.1074/jbc.m405465200
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发表时间：
2004-11-05
影响因子：
4.8
通讯作者：
Verdaguer, N
中科院分区：
文献类型：
--
作者：
Ferrer-Orta, C;Arias, A;Verdaguer, N
小核糖核酸病毒的基因组复制由病毒编码的RNA依赖性RNA聚合酶（称为3D）催化。这种酶在宿主细胞的细胞质中与其他病毒蛋白和可能的宿主蛋白一起执行这一操作。口蹄疫病毒是最重要的动物病原体之一，其3D聚合酶的晶体结构已被确定为无配体的，并与模板引物RNA十核苷酸结合。该酶在特征性的手指、手掌和拇指亚结构域中折叠，并存在包围活性位点的NH 2-末端片段。在复合物中，几个保守的氨基酸侧链与模板引物结合，可能介导RNA合成的起始。该结构为研究RNA复制和设计抗病毒化合物提供了重要信息。
Genome replication in picornaviruses is catalyzed by a virally encoded RNA-dependent RNA polymerase, termed 3D. The enzyme performs this operation, together with other viral and probably host proteins, in the cytoplasm of their host cells. The crystal structure of the 3D polymerase of foot-and-mouth disease virus, one of the most important animal pathogens, has been determined unliganded and bound to a template-primer RNA decanucleotide. The enzyme folds in the characteristic fingers, palm and thumb subdomains, with the presence of an NH2-terminal segment that encircles the active site. In the complex, several conserved amino acid side chains bind to the template-primer, likely mediating the initiation of RNA synthesis. The structure provides essential information for studies on RNA replication and the design of antiviral compounds.