中国病毒学2023，Vol.38Issue(4) ：531-540.DOI:10.1016/j.virs.2023.05.002

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

Xiang Fang Guoliang Lu Yanchun Deng Sa Yang Chunsheng Hou Peng Gong
中国病毒学2023，Vol.38Issue(4) ：531-540.DOI:10.1016/j.virs.2023.05.002
✕
  • NETL
  • NSTL
  • 万方数据

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

Xiang Fang 1Guoliang Lu 2Yanchun Deng 3Sa Yang 4Chunsheng Hou 3Peng Gong5
扫码查看

作者信息

  • 1. Key Laboratory of Special Pathogens and Biosafety,Wuhan Institute of Virology,Chinese Academy of Sciences,Wuhan,430207,China;University of Chinese Academy of Sciences,Beijing,100049,China
  • 2. Key Laboratory of Special Pathogens and Biosafety,Wuhan Institute of Virology,Chinese Academy of Sciences,Wuhan,430207,China
  • 3. Institute of Bast Fiber Crops,Chinese Academy of Agricultural Sciences,Changsha,410205,China
  • 4. Institute of Apicultural Research,Chinese Academy of Agricultural Sciences,Beijing,100193,China
  • 5. Key Laboratory of Special Pathogens and Biosafety,Wuhan Institute of Virology,Chinese Academy of Sciences,Wuhan,430207,China;University of Chinese Academy of Sciences,Beijing,100049,China;Hubei Jiangxia Laboratory,Wuhan,430207,China
  • 折叠

Abstract

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-res-idue 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 Δ85 and Δ40,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 Δ40 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.

Key words

Israeli acute paralysis virus(IAPV)/Poliovirus/RNA-dependent RNA polymerase(RdRP)/Crystal structure/Catalytic motif

引用本文复制引用

基金项目

National Natural Science Foundation of China(31802147)

National Natural Science Foundation of China(31572471)

National Natural Science Foundation of China(31811530276)

National Key Research and Development Program of China(2018YFA0507200)

Agricultural Science and Technology Innovation Program(CAAS-ASTIP-2023-IBFC)

Creative Research Group Program of Natural Science Foundation of Hubei Province(2022CFA021)

Central Public-Interest Scientific Institution Basal Research Fund(Y2021YJ25)

Key Biosafety Science and Technology Program of Hubei Jiangxia Laboratory(JXBS001)

出版年

2023
中国病毒学
中国科学院武汉病毒研究所，中国微生物学会

中国病毒学

CSTPCDCSCD
影响因子：0.393
ISSN：1674-0769
参考文献量54
段落导航相关论文