6M71
SARS-Cov-2 RNA-dependent RNA polymerase in complex with cofactors
Summary for 6M71
Entry DOI | 10.2210/pdb6m71/pdb |
EMDB information | 30127 |
Descriptor | RNA-directed RNA polymerase, Non-structural protein 7, Non-structural protein 8 (3 entities in total) |
Functional Keywords | covid-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 source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) More |
Total number of polymer chains | 4 |
Total formula weight | 161217.36 |
Authors | |
Primary citation | Gao, 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: 32277040DOI: 10.1126/science.abb7498 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
Download full validation report
