Structural and Biochemical Characterization of the nsp12-nsp7-nsp8 Core Polymerase Complex from SARS-CoV-2.

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ID: 107765
2020
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Abstract
The ongoing global pandemic of coronavirus disease 2019 (COVID-19) has caused a huge number of human deaths. Currently, there are no specific drugs or vaccines available for this virus (SARS-CoV-2). The viral polymerase is a promising antiviral target. Here, we describe the near-atomic-resolution structure of the SARS-CoV-2 polymerase complex consisting of the nsp12 catalytic subunit and nsp7-nsp8 cofactors. This structure highly resembles the counterpart of SARS-CoV with conserved motifs for all viral RNA-dependent RNA polymerases and suggests a mechanism of activation by cofactors. Biochemical studies reveal reduced activity of the core polymerase complex and lower thermostability of individual subunits of SARS-CoV-2 compared with SARS-CoV. These findings provide important insights into RNA synthesis by coronavirus polymerase and indicate adaptation of SARS-CoV-2 toward humans with a relatively lower body temperature than the natural bat hosts.
Reference Key
peng2020structuralcell Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Peng, Qi;Peng, Ruchao;Yuan, Bin;Zhao, Jingru;Wang, Min;Wang, Xixi;Wang, Qian;Sun, Yan;Fan, Zheng;Qi, Jianxun;Gao, George F;Shi, Yi;
Journal Cell reports
Year 2020
DOI
S2211-1247(20)30754-3
URL
Keywords
polymerase cryo-em sars-cov-2 rna synthesis cofactors non-structural proteins

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