Structural basis for RNA replication by the SARS-CoV-2 polymerase

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Structural basis for RNA replication by the SARS-CoV-2 polymeraseCryo-EM structures of the SARS-CoV-2 RNA polymerase in complexes with RNA, before and after RNA translocation, reveals structural rearrangements that the RNA dependent RNA polymerase (RdRp) nsp12 and its cofactors (nsp7 and nsp8) undergo to accommodate nucleic acid binding. Further insights into how the complex is inhibited by remdesivir, and into the primase to polymerase transition, are also presented.Cryo-EM structures of the SARS-CoV-2 RNA polymerase in complexes with RNA, before and after RNA translocation, reveals structural rearrangements that the RNA dependent RNA polymerase (RdRp) nsp12 and its cofactors (nsp7 and nsp8) undergo to accommodate nucleic acid binding. Further insights into how the complex is inhibited by remdesivir, and into the primase to polymerase transition, are also presented.Quan Wang, Jiqin Wu, Haofeng Wang, Yan Gao, Qiaojie Liu, An Mu, Wenxin Ji, Liming Yan, Yan Zhu, Chen Zhu, Xiang Fang, Xiaobao Yang, Yucen Huang, Hailong Gao, Fengjiang Liu, Ji Ge, Qianqian Sun, Xiuna Yang, Wenqing Xu, Zhijie Liu, Haitao Yang, Zhiyong Lou, Biao Jiang, Luke W. Guddat, Peng Gong, Zihe Raohttps://secure.jbs.elsevierhealth.com/action/getSharedSiteSession?redirect=https%3A%2F%2Fwww.cell.com%2Fcell%2Ffulltext%2FS0092-8674%2820%2930629-2%3Frss%3Dyes&rc=0http://www.cell.com/cell/inpress.rssCellCell RSS feed.Wireless News CampaignMay 23, 2020

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