ArticleMolecular cell2023
Structural and functional insights into the enzymatic plasticity of the SARS-CoV-2 NiRAN domain.
Article in Molecular cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Structural and Mechanistic Perspectives on SARS-CoV-2 Nonstructural Protein 14-Mediated Cap Formation and Drug Discovery.Microorganisms · 2026Review
- Article
- Polypeptide encoded by the -1 PRF signal of SARS-CoV-2 controls multiple enzymatic activities of the viral NiRAN domain.NAR molecular medicine · 2025Article
- Development of GFP-expressing infectious clones for PRRSV using TAR cloning for antiviral drug screening.Npj viruses · 2025Article
- The mechanism for GTP-mediated RNA capping by the SARS-CoV-2 NiRAN domain remains unresolved.Cell · 2025Article
- Meeting report of the 37th International Conference on Antiviral Research in Gold Coast, Australia, May 20-24, 2024, organized by the International Society for Antiviral Research.Antiviral research · 2024Article
- Article
- Nanobody against SARS-CoV-2 non-structural protein Nsp9 inhibits viral replication in human airway epithelia.Molecular therapy. Nucleic acids · 2024Article
- Inhibition of SARS-CoV-2 Nsp9 ssDNA-Binding Activity and Cytotoxic Effects on H838, H1975, and A549 Human Non-Small Cell Lung Cancer Cells: Exploring the Potential ofInternational journal of molecular sciences · 2024Article
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Authors and funding
10 authors.
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Abstract
The enzymatic activity of the SARS-CoV-2 nidovirus RdRp-associated nucleotidyltransferase (NiRAN) domain is essential for viral propagation, with three distinct activities associated with modification of the nsp9 N terminus, NMPylation, RNAylation, and deRNAylation/capping via a GDP-polyribonucleotidyltransferase reaction. The latter two activities comprise an unconventional mechanism for initiating viral RNA 5' cap formation, while the role of NMPylation is unclear. The structural mechanisms for these diverse enzymatic activities have not been properly delineated. Here, we determine high-resolution cryoelectron microscopy (cryo-EM) structures of catalytic intermediates for the NMPylation and deRNAylation/capping reactions, revealing diverse nucleotide binding poses and divalent metal ion coordination sites to promote its repertoire of activities. The deRNAylation/capping structure explains why GDP is a preferred substrate for the capping reaction over GTP. Altogether, these findings enhance our understanding of the promiscuous coronaviral NiRAN domain, a therapeutic target, and provide an accurate structural platform for drug development.
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