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

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Virologica Sinica 2023年第4期38卷 531-540页

作者： Xiang Fang Guoliang Lu Yanchun Deng Sa Yang Chunsheng Hou Peng Gong Key Laboratory of Special Pathogens and Biosafety Wuhan Institute of VirologyChinese Academy of SciencesWuhan430207China Institute of Bast Fiber Crops Chinese Academy of Agricultural SciencesChangsha410205China University of Chinese Academy of Sciences Beijing100049China Institute of Apicultural Research Chinese Academy of Agricultural SciencesBeijing100193China Hubei Jiangxia Laboratory Wuhan430207China

The Dicistroviridae is a virus family that includes many insect *** viruses contain a positive-sense RNA genome that is replicated by the virally encoded RNA-dependent RNA polymerase(RdRP)also named 3D^(pol).Compared with the Picornaviridae RdRPs such as poliovirus(PV)3D^(pol),the Dicistroviridae representative Israeli acute paralysis virus(IAPV)3D^(pol) has an additional N-terminal extension(NE)region that is about 40-residue in *** date,both the structure and catalytic mechanism of the Dicistroviridae RdRP have remain *** we reported crystal structures of two truncated forms of IAPV 3D^(pol),namelyΔ85 andΔ40,both missing the NE region,and the 3D^(pol) protein in these structures exhibited three conformational *** palm and thumb domains of these IAPV 3D^(pol) structures are largely consistent with those of the PV 3D^(pol) ***,in all structures,the RdRP fingers domain is partially disordered,while different conformations of RdRP substructures and interactions between them are also *** particular,a large-scale conformational change occurred in the motif B-middle finger region in one protein chain of theΔ40 structure,while a previously documented alternative conformation of motif A was observed in all IAPV *** 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.

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

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