ArticleThe EMBO journal2007
Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferase.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 80 citations in OpenAlex.
- Vaccinia Virus Capping Enzyme Subunit D12 Is Differentially Required for Viral Replication in Different Cell Lines and Gastrointestinal Organoids.Journal of medical virology · 2026Article
- Structure and function of the RNA polymerase complex of Borna disease virus, a nuclear-replicating non-segmented negative-strand RNA virus.Nucleic acids research · 2026Article
- Structural basis for sensitivity and acquired resistance of fungal cap guanine-N7 methyltransferases to the antifungal antibiotic sinefungin.Nucleic acids research · 2025Article
- Directed evolution of an orthogonal transcription engine for programmable gene expression in eukaryotes.iScience · 2025Article
- Structural basis of the monkeypox virus mRNA cap N7 methyltransferase complex.Emerging microbes & infections · 2024Article
- Directed evolution of an orthogonal transcription engine for programmable gene expression in eukaryotes.bioRxiv : the preprint server for biology · 2024Article
- Biochemical characterization of mRNA capping enzyme from Faustovirus.RNA (New York, N.Y.) · 2023Article
- Characterization, Directed Evolution, and Targeting of DNA Virus-Encoded RNA Capping Enzymes Using Phenotypic Yeast Platforms.ACS chemical biology · 2023Article
- Versatile strategy using vaccinia virus-capping enzyme to synthesize functional 5' cap-modified mRNAs.Nucleic acids research · 2023Article
- Structural basis and dynamics of Chikungunya alphavirus RNA capping by nsP1 capping pores.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Biochemistry of the Respiratory Syncytial Virus L Protein Embedding RNA Polymerase and Capping Activities.Viruses · 2023Review
- Review
- Evolutionary dissection of monkeypox virus: Positive Darwinian selection drives the adaptation of virus-host interaction proteins.Frontiers in cellular and infection microbiology · 2022Article
- Enzymatic Assays to Explore Viral mRNA Capping Machinery.Chembiochem : a European journal of chemical biology · 2021Review
- 5'-Cap sequestration is an essential determinant of HIV-1 genome packaging.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure and Biochemical Characteristic of the Methyltransferase (MTase) Domain of RNA Capping Enzyme from African Swine Fever Virus.Journal of virology · 2021Article
- Article
- HIV-1 spliced RNAs display transcription start site bias.RNA (New York, N.Y.) · 2020Article
- The C-Terminal Domain of the Sudan Ebolavirus L Protein Is Essential for RNA Binding and Methylation.Journal of virology · 2020Article
- Structural basis for transcriptional start site control of HIV-1 RNA fate.Science (New York, N.Y.) · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The vaccinia virus mRNA capping enzyme is a multifunctional heterodimeric protein associated with the viral polymerase that both catalyses the three steps of mRNA capping and regulates gene transcription. The structure of a subcomplex comprising the C-terminal N7-methyl-transferase (MT) domain of the large D1 subunit, the stimulatory D12 subunit and bound S-adenosyl-homocysteine (AdoHcy) has been determined at 2.7 A resolution and reveals several novel features of the poxvirus capping enzyme. The structure shows for the first time the critical role played by the proteolytically sensitive N-terminus of the MT domain in binding the methyl donor and in catalysis. In addition, the poxvirus enzyme has a completely unique mode of binding of the adenosine moiety of AdoHcy, a feature that could be exploited for design of specific anti-poxviral compounds. The structure of the poxvirus-specific D12 subunit suggests that it was originally an RNA cap 2'O-MT that has evolved to a catalytically inactive form that has been retained for D1 stabilisation and MT activity enhancement through an allosteric mechanism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.