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7BTF

SARS-CoV-2 RNA-dependent RNA polymerase in complex with cofactors in reduced condition

Summary for 7BTF
Entry DOI10.2210/pdb7btf/pdb
EMDB information30178
DescriptorRNA-directed RNA polymerase, Non-structural protein 7, Non-structural protein 8, ... (4 entities in total)
Functional Keywordscovid-19, 2019-ncov, sars-cov-2, virus, rdrp, nsp12, nsp7, nsp8, rtc, cryo-em, viral protein, rna polymerase, drug target, antiviral, replication transcription complex
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV)
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Total number of polymer chains4
Total formula weight161348.18
Authors
Gao, Y.,Yan, L.,Huang, Y.,Liu, F.,Cao, L.,Wang, T.,Wang, Q.,Lou, Z.,Rao, Z. (deposition date: 2020-04-01, release date: 2020-04-08, Last modification date: 2024-03-27)
Primary citationGao, Y.,Yan, L.,Huang, Y.,Liu, F.,Zhao, Y.,Cao, L.,Wang, T.,Sun, Q.,Ming, Z.,Zhang, L.,Ge, J.,Zheng, L.,Zhang, Y.,Wang, H.,Zhu, Y.,Zhu, C.,Hu, T.,Hua, T.,Zhang, B.,Yang, X.,Li, J.,Yang, H.,Liu, Z.,Xu, W.,Guddat, L.W.,Wang, Q.,Lou, Z.,Rao, Z.
Structure of the RNA-dependent RNA polymerase from COVID-19 virus.
Science, 368:779-782, 2020
Cited by
PubMed Abstract: A novel coronavirus [severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2)] outbreak has caused a global coronavirus disease 2019 (COVID-19) pandemic, resulting in tens of thousands of infections and thousands of deaths worldwide. The RNA-dependent RNA polymerase [(RdRp), also named nsp12] is the central component of coronaviral replication and transcription machinery, and it appears to be a primary target for the antiviral drug remdesivir. We report the cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9-angstrom resolution. In addition to the conserved architecture of the polymerase core of the viral polymerase family, nsp12 possesses a newly identified β-hairpin domain at its N terminus. A comparative analysis model shows how remdesivir binds to this polymerase. The structure provides a basis for the design of new antiviral therapeutics that target viral RdRp.
PubMed: 32277040
DOI: 10.1126/science.abb7498
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.95 Å)
Structure validation

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