数字农科院2.0

Unusual substructure conformations observed in crystal structures of a dicistrovirus RNA-dependent RNA polymerase suggest contribution of the N-terminal extension in proper folding

文献类型： 外文期刊

作者： Fang, Xiang;Lu, Guoliang;Deng, Yanchun;Yang, Sa;Hou, Chunsheng;Gong, Peng

作者机构：

关键词： Israeli acute paralysis virus (IAPV);Poliovirus;RNA-dependent RNA polymerase (RdRP);Crystal structure;Catalytic motif

期刊名称： VIROLOGICA SINICA

ISSN： 1674-0769

年卷期： 2023 年 38 卷 4 期

页码：

收录情况： SCIE（2023版） ; ; CSCD（2023-2024年度） ; ; 科技核心（2023版）

摘要： The Dicistroviridae is a virus family that includes many insect pathogens. These viruses contain a positive-sense RNA genome that is replicated by the virally encoded RNA-dependent RNA polymerase (RdRP) also named 3Dpol. Compared with the Picornaviridae RdRPs such as poliovirus (PV) 3Dpol, the Dicistroviridae representative Israeli acute paralysis virus (IAPV) 3Dpol has an additional N-terminal extension (NE) region that is about 40-residue in length. To date, both the structure and catalytic mechanism of the Dicistroviridae RdRP have remain elusive. Here we reported crystal structures of two truncated forms of IAPV 3Dpol, namely & UDelta;85 and & UDelta;40, both missing the NE region, and the 3Dpol protein in these structures exhibited three conformational states. The palm and thumb domains of these IAPV 3Dpol structures are largely consistent with those of the PV 3Dpol structures. However, in all structures, the RdRP fingers domain is partially disordered, while different conformations of RdRP substructures and interactions between them are also present. In particular, a large-scale conformational change occurred in the motif B-middle finger region in one protein chain of the & UDelta;40 structure, while a previously documented alternative conformation of motif A was observed in all IAPV structures. These experimental data on one hand show intrinsic conformational variances of RdRP substructures, and on the other hand suggest possible contribution of the NE region in proper RdRP folding in IAPV.

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