7BW4

Structure of the RNA-dependent RNA polymerase from SARS-CoV-2

Summary for 7BW4

• Entry DOI: 10.2210/pdb7bw4/pdb
• EMDB information: 30226
• Descriptor: RNA-directed RNA polymerase, Non-structural protein 8, Non-structural protein 7, ... (4 entities in total)
• Functional Keywords: sars-cov-2, polymerase, cryo-em, replication
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV); More
• Total number of polymer chains: 4
• Total formula weight: 159032.72

Authors

Peng, Q.,Peng, R.,Shi, Y. (deposition date: 2020-04-13, release date: 2020-05-27, Last modification date: 2024-03-27)

Primary citation

Peng, Q.,Peng, R.,Yuan, B.,Zhao, J.,Wang, M.,Wang, X.,Wang, Q.,Sun, Y.,Fan, Z.,Qi, J.,Gao, G.F.,Shi, Y.
Structural and Biochemical Characterization of the nsp12-nsp7-nsp8 Core Polymerase Complex from SARS-CoV-2.
Cell Rep, 31:107774-107774, 2020

PubMed 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.

PubMed: 32531208
DOI: 10.1016/j.celrep.2020.107774

Experimental method

ELECTRON MICROSCOPY (3.7 Å)