Structural insights into replication initiation and elongation processes by the FMDV RNA-dependent RNA polymerase
Structural insights into replication initiation and elongation processes by the FMDV RNA-dependent RNA polymerase
复制标题
DOI：
10.1016/j.sbi.2009.10.016
复制
发表时间：
2009-12-01
影响因子：
6.8
通讯作者：
Verdaguer, Nuria
中科院分区：
文献类型：
--
作者：
Ferrer-Orta, Cristina;Agudo, Ruben;Verdaguer, Nuria
RNA依赖的RNA聚合酶(RdRPs)在转录和病毒基因组复制中发挥着重要作用。在小核糖核酸病毒中，这些功能是由病毒编码的RdRP催化的，称为3D。聚合酶3D还催化UMP与小蛋白VPG上的酪氨酸的共价连接。然后，尿苷酰化的VPG作为启动RNA合成的蛋白质引物。口蹄疫病毒(FMDV)3D催化复合体的7种不同晶体结构加深了我们对模板和引物识别、VPG尿苷基化以及rNTP结合和催化的理解。这些结构信息为RNA复制的保真度提供了新的见解，并为抗病毒化合物的设计提供了新的见解。
RNA-dependent RNA polymerases (RdRPs) play central roles in both transcription and viral genome replication. In picornaviruses, these functions are catalyzed by the virally encoded RdRP, termed 3D. Polymerase 3D also catalyzes the covalent linkage of UMP to a tyrosine on the small protein VPg. Uridylylated VPg then serves as a protein primer for the initiation of RNA synthesis. Seven different crystal structures of foot-and-mouth disease virus (FMDV) 3D catalytic complexes have enhanced our understanding of template and primer recognition, VPg uridylylation, and rNTP binding and catalysis. Such structural information is providing new insights into the fidelity of RNA replication, and for the design of antiviral compounds.