Structure of the RNA-dependent RNA polymerase from COVID-19 virus

A novel coronavirus [severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2)] outbreak has caused a global coronavirus disease 2019 (COVID-19) pandemic, resulting in tens of thousands of infections and thousands of deaths worldwide. The RNA-dependent RNA polymerase [(RdRp), also named nsp12] is...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 2020-05, Vol.368 (6492), p.779-782
Hauptverfasser:	Gao, Yan, Yan, Liming, Huang, Yucen, Liu, Fengjiang, Zhao, Yao, Cao, Lin, Wang, Tao, Sun, Qianqian, Ming, Zhenhua, Zhang, Lianqi, Ge, Ji, Zheng, Litao, Zhang, Ying, Wang, Haofeng, Zhu, Yan, Zhu, Chen, Hu, Tianyu, Hua, Tian, Zhang, Bing, Yang, Xiuna, Li, Jun, Yang, Haitao, Liu, Zhijie, Xu, Wenqing, Guddat, Luke W, Wang, Quan, Lou, Zhiyong, Rao, Zihe
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Monophosphate - analogs & derivatives Adenosine Monophosphate - metabolism Adenosine Monophosphate - pharmacology Alanine - analogs & derivatives Alanine - metabolism Alanine - pharmacology Antiviral Agents - metabolism Antiviral Agents - pharmacology Betacoronavirus - enzymology Biochem Catalytic Domain Chemical synthesis Cofactors Comparative analysis Coronaviridae Coronavirus RNA-Dependent RNA Polymerase Coronaviruses COVID-19 Cryoelectron Microscopy DNA-directed RNA polymerase Drug Design Electron microscopy Microbio Microscopy Models, Molecular Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism Multiprotein Complexes - ultrastructure Nucleotide analogs Nucleotides Pandemics Protein Conformation, beta-Strand Protein Domains Replication Respiratory diseases RNA polymerase RNA viruses RNA-Dependent RNA Polymerase - antagonists & inhibitors RNA-Dependent RNA Polymerase - chemistry RNA-Dependent RNA Polymerase - metabolism RNA-Dependent RNA Polymerase - ultrastructure RNA-directed RNA polymerase SARS-CoV-2 Severe acute respiratory syndrome Severe acute respiratory syndrome coronavirus 2 Transcription Viral diseases Viral Nonstructural Proteins - antagonists & inhibitors Viral Nonstructural Proteins - chemistry Viral Nonstructural Proteins - metabolism Viral Nonstructural Proteins - ultrastructure Viruses
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Zusammenfassung:	A novel coronavirus [severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2)] outbreak has caused a global coronavirus disease 2019 (COVID-19) pandemic, resulting in tens of thousands of infections and thousands of deaths worldwide. The RNA-dependent RNA polymerase [(RdRp), also named nsp12] is the central component of coronaviral replication and transcription machinery, and it appears to be a primary target for the antiviral drug remdesivir. We report the cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9-angstrom resolution. In addition to the conserved architecture of the polymerase core of the viral polymerase family, nsp12 possesses a newly identified β-hairpin domain at its N terminus. A comparative analysis model shows how remdesivir binds to this polymerase. The structure provides a basis for the design of new antiviral therapeutics that target viral RdRp.
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.abb7498