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; Rao, Zihe1,2,3,4
2019-07-09
Source PublicationNUCLEIC ACIDS RESEARCH
ISSN0305-1048
Volume47Issue:12Pages:6538-6550
Status已发表
DOI10.1093/nar/gkz409
AbstractTo 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.
Indexed BySCI
Language英语
Funding ProjectNational 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 Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemistry & Molecular Biology
WOS IDWOS:000475891900045
PublisherOXFORD UNIV PRESS
WOS KeywordENZYMATIC-ACTIVITIES ; SARS ; PROTEINS ; HELICASES ; APTAMERS ; SEQUENCE ; SERVER ; TOOLS ; UPF1
Original Document TypeArticle
Citation statistics
Cited Times:1[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://kms.shanghaitech.edu.cn/handle/2MSLDSTB/61053
CollectioniHuman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
Corresponding AuthorRao, Zihe
Affiliation1.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
Corresponding Author AffilicationShanghai Institute for Advanced Immunochemical Studies;  iHuman Institute
Recommended Citation
GB/T 7714
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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