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7EIZ

Coupling of N7-methyltransferase and 3'-5' exoribonuclease with SARS-CoV-2 polymerase reveals mechanisms for capping and proofreading

This is a non-PDB format compatible entry.
Summary for 7EIZ
Entry DOI10.2210/pdb7eiz/pdb
EMDB information31146
DescriptorRNA-directed RNA polymerase, ZINC ION, MAGNESIUM ION, ... (11 entities in total)
Functional Keywordsviral protein-rna complex, viral protein/rna
Biological sourceSevere acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
More
Total number of polymer chains11
Total formula weight398007.74
Authors
Yan, L.,Yang, Y.X.,Li, M.Y.,Zhang, Y.,Zheng, L.T.,Ge, J.,Huang, Y.C.,Liu, Z.Y.,Wang, T.,Gao, S.,Zhang, R.,Huang, Y.Y.,Guddat, L.W.,Gao, Y.,Rao, Z.H.,Lou, Z.Y. (deposition date: 2021-04-01, release date: 2021-09-22, Last modification date: 2023-07-26)
Primary citationYan, L.,Yang, Y.,Li, M.,Zhang, Y.,Zheng, L.,Ge, J.,Huang, Y.C.,Liu, Z.,Wang, T.,Gao, S.,Zhang, R.,Huang, Y.Y.,Guddat, L.W.,Gao, Y.,Rao, Z.,Lou, Z.
Coupling of N7-methyltransferase and 3'-5' exoribonuclease with SARS-CoV-2 polymerase reveals mechanisms for capping and proofreading
Cell, 184:3474-3485.e11, 2021
Cited by
PubMed Abstract: The capping of mRNA and the proofreading play essential roles in SARS-CoV-2 replication and transcription. Here, we present the cryo-EM structure of the SARS-CoV-2 replication-transcription complex (RTC) in a form identified as Cap(0)-RTC, which couples a co-transcriptional capping complex (CCC) composed of nsp12 NiRAN, nsp9, the bifunctional nsp14 possessing an N-terminal exoribonuclease (ExoN) and a C-terminal N7-methyltransferase (N7-MTase), and nsp10 as a cofactor of nsp14. Nsp9 and nsp12 NiRAN recruit nsp10/nsp14 into the Cap(0)-RTC, forming the N7-CCC to yield cap(0) (GpppA) at 5' end of pre-mRNA. A dimeric form of Cap(0)-RTC observed by cryo-EM suggests an in trans backtracking mechanism for nsp14 ExoN to facilitate proofreading of the RNA in concert with polymerase nsp12. These results not only provide a structural basis for understanding co-transcriptional modification of SARS-CoV-2 mRNA but also shed light on how replication fidelity in SARS-CoV-2 is maintained.
PubMed: 34143953
DOI: 10.1016/j.cell.2021.05.033
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY
Structure validation

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