Delicate structural coordination of the Severe Acute Respiratory Syndrome coronavirus Nsp13 upon ATP hydrolysis
Jia, Zhihui1; Yan, Liming1; Ren, Zhilin2; Wu, Lijie3,4; Wang, Jin5; Guo, Jing6; Zheng, Litao1; Ming, Zhenhua7; Zhang, Lianqi1; Lou, Zhiyong1
2019-07-09
发表期刊NUCLEIC ACIDS RESEARCH
ISSN0305-1048
卷号47期号:12页码:6538-6550
发表状态已发表
DOI10.1093/nar/gkz409
摘要To date, an effective therapeutic treatment that confers strong attenuation toward coronaviruses (CoVs) remains elusive. Of all the potential drug targets, the helicase of CoVs is considered to be one of the most important. Here, we first present the structure of the full-length Nsp13 helicase of SARS-CoV (SARS-Nsp13) and investigate the structural coordination of its five domains and how these contribute to its translocation and unwinding activity. A translocation model is proposed for the Upf1-like helicase members according to three different structural conditions in solution characterized through H/D exchange assay, including substrate state (SARS-Nsp13-dsDNA bound with AMPPNP), transition state (bound with ADP-AlF4-) and product state (bound with ADP). We observed that the beta 19-beta 20 loop on the 1A domain is involved in unwinding process directly. Furthermore, we have shown that the RNA dependent RNA polymerase (RdRp), SARS-Nsp12,can enhance the helicase activity of SARS-Nsp13 through interacting with it directly. The interacting regions were identified and can be considered common across CoVs, which provides new insights into the Replication and Transcription Complex (RTC) of CoVs.
收录类别SCI ; SCIE
语种英语
资助项目National Natural Science Foundation of China[81330036] ; National Natural Science Foundation of China[31570717] ; National Natural Science Foundation of China[81621005] ; National Natural Science Foundation of China[81520108019]
WOS研究方向Biochemistry & Molecular Biology
WOS类目Biochemistry & Molecular Biology
WOS记录号WOS:000475891900045
出版者OXFORD UNIV PRESS
WOS关键词ENZYMATIC-ACTIVITIES ; SARS ; PROTEINS ; HELICASES ; APTAMERS ; SEQUENCE ; SERVER ; TOOLS ; UPF1
原始文献类型Article
引用统计
文献类型期刊论文
条目标识符https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/61053
专题iHuman研究所_科学装置(X)_膜蛋白同步辐射线站
免疫化学研究所_特聘教授组_饶子和组
通讯作者Rao, Zihe
作者单位1.Tsinghua Univ, Sch Med, Struct Biol Lab, Beijing 100084, Peoples R China
2.Nankai Univ, Coll Life Sci, State Key Lab Med Chem Biol, Tianjin 300353, Peoples R China
3.ShanghaiTech Univ, Shanghai Inst Adv Immunochem Studies, Shanghai 201210, Peoples R China
4.ShanghaiTech Univ, IHuman Inst, Shanghai 201210, Peoples R China
5.Sichuan Univ, West China Hosp, State Key Lab Biotherapy, Chengdu 610041, Peoples R China
6.Tsinghua Univ, Prot Chem Facil, Ctr Biomed Anal, Beijing 100084, Peoples R China
7.Guangxi Univ, Coll Life Sci & Technol, State Key Lab Conservat & Utilizat Subtrop Agrobi, Nanning, Peoples R China
通讯作者单位免疫化学研究所;  iHuman研究所
推荐引用方式
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Jia, Zhihui,Yan, Liming,Ren, Zhilin,et al. Delicate structural coordination of the Severe Acute Respiratory Syndrome coronavirus Nsp13 upon ATP hydrolysis[J]. NUCLEIC ACIDS RESEARCH,2019,47(12):6538-6550.
APA Jia, Zhihui.,Yan, Liming.,Ren, Zhilin.,Wu, Lijie.,Wang, Jin.,...&Rao, Zihe.(2019).Delicate structural coordination of the Severe Acute Respiratory Syndrome coronavirus Nsp13 upon ATP hydrolysis.NUCLEIC ACIDS RESEARCH,47(12),6538-6550.
MLA Jia, Zhihui,et al."Delicate structural coordination of the Severe Acute Respiratory Syndrome coronavirus Nsp13 upon ATP hydrolysis".NUCLEIC ACIDS RESEARCH 47.12(2019):6538-6550.
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