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TitleStructural and Biochemical Characterization of the nsp12-nsp7-nsp8 Core Polymerase Complex from SARS-CoV-2.
Journal, issue, pagesCell Rep, Vol. 31, Issue 11, Page 107774, Year 2020
Publish dateJun 16, 2020
AuthorsQi Peng / Ruchao Peng / Bin Yuan / Jingru Zhao / Min Wang / Xixi Wang / Qian Wang / Yan Sun / Zheng Fan / Jianxun Qi / George F Gao / Yi Shi /
PubMed AbstractThe 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 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.
External linksCell Rep / PubMed:32531208 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

30226

7bw4

EMDB-30226, PDB-7bw4:
Structure of the RNA-dependent RNA polymerase from SARS-CoV-2
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • SARS coronavirus
  • severe acute respiratory syndrome coronavirus 2
KeywordsREPLICATION / SARS-CoV-2 / Polymerase / cryo-EM

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