Journal
CELL REPORTS
Volume 31, Issue 11, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2020.107774
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Funding
- Strategic Priority Research Program of the CAS [XDB29010000]
- National Science and Technology Major Project [2018ZX09711003, 2018ZX10101004]
- National Key Research and Development Program of China [2020YFC0845900]
- National Natural Science Foundation of China (NSFC) [81802007, 82041016, 81871658, 81802010]
- Bill and Melinda Gates Foundation
- Young Elite Scientist Sponsorship Program (YESS) of the China Association for Science and Technology (CAST) [2018QNRC001]
- Excellent Young Scientist Program from the NSFC [81622031]
- Youth Innovation Promotion Association of CAS [2015078]
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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 SARSCoV-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.
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