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Delicate structural coordination of the Severe Acute Respiratory Syndrome coronavirus Nsp13 upon ATP hydrolysis | |
2019-07-09 | |
发表期刊 | NUCLEIC ACIDS RESEARCH (IF:16.6[JCR-2023],16.1[5-Year]) |
ISSN | 0305-1048 |
卷号 | 47期号:12页码:6538-6550 |
发表状态 | 已发表 |
DOI | 10.1093/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 | 正在获取...
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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 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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