Evidence map›Paper›PMID 36298761›Full record

ArticleViruses2022

The Vaccinia Virus DNA Helicase Structure from Combined Single-Particle Cryo-Electron Microscopy and AlphaFold2 Prediction.

Stephanie Hutin, Wai Li Ling, Nicolas Tarbouriech, Guy Schoehn, Clemens Grimm, Utz Fischer, Wim P Burmeister

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

16 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
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  6. Structural basis of DNA replication fidelity of the Mpox virus.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Methods to Study Poxvirus Structures by Cryo-EM Imaging Modalities.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  8. Article
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  12. Article
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  15. AlphaFold2 and its applications in the fields of biology and medicine.Signal transduction and targeted therapy · 2023
    Review
  16. Article
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

7 authors at 2 institutions in 2 countries.

Stephanie HutinInstitut de Biologie Structurale (IBS), Université Grenoble Alpes (UGA), Commissariat à l'Energie Atomique et aux Energies Alternatives (CEA), Centre National de la Recherche Scientifique (CNRS), 38000 Grenoble, France.
Wai Li LingInstitut de Biologie Structurale (IBS), Université Grenoble Alpes (UGA), Commissariat à l'Energie Atomique et aux Energies Alternatives (CEA), Centre National de la Recherche Scientifique (CNRS), 38000 Grenoble, France.
Nicolas TarbouriechInstitut de Biologie Structurale (IBS), Université Grenoble Alpes (UGA), Commissariat à l'Energie Atomique et aux Energies Alternatives (CEA), Centre National de la Recherche Scientifique (CNRS), 38000 Grenoble, France.ORCID 0000-0002-0206-3959
Guy SchoehnInstitut de Biologie Structurale (IBS), Université Grenoble Alpes (UGA), Commissariat à l'Energie Atomique et aux Energies Alternatives (CEA), Centre National de la Recherche Scientifique (CNRS), 38000 Grenoble, France.ORCID 0000-0002-1459-3201
Clemens GrimmBiozentrum, University of Würzburg, 97070 Würzburg, Germany.
Utz FischerBiozentrum, University of Würzburg, 97070 Würzburg, Germany.
Wim P BurmeisterInstitut de Biologie Structurale (IBS), Université Grenoble Alpes (UGA), Commissariat à l'Energie Atomique et aux Energies Alternatives (CEA), Centre National de la Recherche Scientifique (CNRS), 38000 Grenoble, France.ORCID 0000-0003-0876-6118
Centre National de la Recherche Scientifique · FRUniversity of Würzburg · DE

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
NIGMS NIH HHS P41 GM103311NIH HHS P41-GM103311
6 · The paper itself

Abstract

Poxviruses are large DNA viruses with a linear double-stranded DNA genome circularized at the extremities. The helicase-primase D5, composed of six identical 90 kDa subunits, is required for DNA replication. D5 consists of a primase fragment flexibly attached to the hexameric C-terminal polypeptide (res. 323-785) with confirmed nucleotide hydrolase and DNA-binding activity but an elusive helicase activity. We determined its structure by single-particle cryo-electron microscopy. It displays an AAA+ helicase core flanked by N- and C-terminal domains. Model building was greatly helped by the predicted structure of D5 using AlphaFold2. The 3.9 Å structure of the N-terminal domain forms a well-defined tight ring while the resolution decreases towards the C-terminus, still allowing the fit of the predicted structure. The N-terminal domain is partially present in papillomavirus E1 and polyomavirus LTA helicases, as well as in a bacteriophage NrS-1 helicase domain, which is also closely related to the AAA+ helicase domain of D5. Using the Pfam domain database, a D5_N domain followed by DUF5906 and Pox_D5 domains could be assigned to the cryo-EM structure, providing the first 3D structures for D5_N and Pox_D5 domains. The same domain organization has been identified in a family of putative helicases from large DNA viruses, bacteriophages, and selfish DNA elements.

Indexed as

DNA PrimaseVaccinia virusCryoelectron MicroscopyDNADNA HelicasesDNA ReplicationNucleotidesDNADNA HelicasesDNA PrimaseNucleotidescryo-electron microscopyDNA helicaseDNA replicationhelicaseorthopoxvirusPfam domainpoxvirusSF3 helicasestructure prediction

Identifiers

PMID36298761
PMCPMC9611036
OpenAlexW4304789266

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.