Evidence map›Paper›PMID 24607143›Full record

ArticleStructure (London, England : 1993)2014

Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus.

Otto J P Kyrieleis, Jonathan Chang, Marcos de la Peña, Stewart Shuman, Stephen Cusack

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.3field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed, 66 citations in OpenAlex.

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  13. Article
  14. A comparative exploration of mRNA capping enzymes.Biotechnology notes (Amsterdam, Netherlands) · 2024
    Article
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  19. Article
  20. Enzymatic Assays to Explore Viral mRNA Capping Machinery.Chembiochem : a European journal of chemical biology · 2021
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Otto J P KyrieleisEuropean Molecular Biology Laboratory, Grenoble Outstation, 6 rue Horowitz, BP 181, 38042 Grenoble Cedex 9, France; University Grenoble Alpes-CNRS-EMBL Unit of Virus Host Cell Interactions, 6 rue Horowitz, BP 181, 38042 Grenoble Cedex 9, France.
Jonathan ChangMolecular Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA.
Marcos de la PeñaEuropean Molecular Biology Laboratory, Grenoble Outstation, 6 rue Horowitz, BP 181, 38042 Grenoble Cedex 9, France.
Stewart ShumanMolecular Biology Program, Sloan-Kettering Institute, New York, NY 10065, USA. Electronic address: s-shuman@ski.mskcc.org.
Stephen CusackEuropean Molecular Biology Laboratory, Grenoble Outstation, 6 rue Horowitz, BP 181, 38042 Grenoble Cedex 9, France; University Grenoble Alpes-CNRS-EMBL Unit of Virus Host Cell Interactions, 6 rue Horowitz, BP 181, 38042 Grenoble Cedex 9, France. Electronic address: cusack@embl.fr.
European Molecular Biology Laboratory · FRKettering University · USCentre National de la Recherche Scientifique · FR

Funding

Viral RNA Modifying EnzymesR01GM042498 · NIGMS · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI SHUMAN, STEWART H · 1989 to 2017
$6.8M
NIGMS NIH HHS GM42498NIGMS NIH HHS R01 GM042498
6 · The paper itself

Abstract

Vaccinia virus capping enzyme is a heterodimer of D1 (844 aa) and D12 (287 aa) polypeptides that executes all three steps in m(7)GpppRNA synthesis. The D1 subunit comprises an N-terminal RNA triphosphatase (TPase)-guanylyltransferase (GTase) module and a C-terminal guanine-N7-methyltransferase (MTase) module. The D12 subunit binds and allosterically stimulates the MTase module. Crystal structures of the complete D1⋅D12 heterodimer disclose the TPase and GTase as members of the triphosphate tunnel metalloenzyme and covalent nucleotidyltransferase superfamilies, respectively, albeit with distinctive active site features. An extensive TPase-GTase interface clamps the GTase nucleotidyltransferase and OB-fold domains in a closed conformation around GTP. Mutagenesis confirms the importance of the TPase-GTase interface for GTase activity. The D1⋅D12 structure complements and rationalizes four decades of biochemical studies of this enzyme, which was the first capping enzyme to be purified and characterized, and provides new insights into the origins of the capping systems of other large DNA viruses.

Indexed as

Catalytic DomainCrystallography, X-RayEvolution, MolecularMethyltransferasesModels, MolecularMultienzyme ComplexesMutationNucleotidyltransferasesPhosphoric Monoester HydrolasesProtein ConformationProtein MultimerizationVaccinia virusViral Proteinscapping enzyme, vaccinia virusMethyltransferasesMultienzyme ComplexesNucleotidyltransferasesPhosphoric Monoester HydrolasesViral Proteins

Identifiers

PMID24607143
PMCPMC4010090
OpenAlexW2151882149

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

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.