ArticleNature communications2017
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 48 citations in OpenAlex.
- Infection cycles of viruses of the phylum Nucleocytoviricota.Nature reviews. Microbiology · 2026Review
- Identification of Repurposed Drugs Against Monkeypox Virus Through Comprehensive Virtual Screening.Biotechnology journal · 2026Article
- AI-driven discovery of antiretroviral drug bictegravir and etravirine as inhibitors against monkeypox and related poxviruses.Communications biology · 2025Article
- Inhibition of monkeypox polymerase holoenzyme and methyltransferase using bioactive compounds of black tea: a computational approach.Scientific reports · 2025Article
- Essential and multifunctional mpox virus E5 helicase-primase in double and single hexamer.Science advances · 2024Article
- Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus.PLoS pathogens · 2024Article
- Structural insight into the assembly and working mechanism of helicase-primase D5 from Mpox virus.Nature structural & molecular biology · 2024Article
- Viral replication organelles: the highly complex and programmed replication machinery.Frontiers in microbiology · 2024Review
- Cryo-EM structures of human monkeypox viral replication complexes with and without DNA duplex.Cell research · 2023Article
- Computational studies on searching potential phytochemicals against DNA polymerase activity of the monkeypox virus.Journal of traditional and complementary medicine · 2023Article
- Article
- Structural basis for the assembly of the DNA polymerase holoenzyme from a monkeypox virus variant.Science advances · 2023Article
- Identification of probable inhibitors for the DNA polymerase of the Monkeypox virus through the virtual screening approach.International journal of biological macromolecules · 2023Article
- Mutations in the monkeypox virus replication complex: Potential contributing factors to the 2022 outbreak.Journal of autoimmunity · 2022Article
- Poxvirus Recombination.Pathogens (Basel, Switzerland) · 2022Review
- Efficient Method for Generating Point Mutations in the Vaccinia Virus Genome Using CRISPR/Cas9.Viruses · 2022Article
- Poxviruses Bearing DNA Polymerase Mutations Show Complex Patterns of Cross-Resistance.Biomedicines · 2022Article
- Selection of Primer-Template Sequences That Bind with Enhanced Affinity to Vaccinia Virus E9 DNA Polymerase.Viruses · 2022Article
- Evaluation of model refinement in CASP14.Proteins · 2021Article
- Assessment of prediction methods for protein structures determined by NMR in CASP14: Impact of AlphaFold2.Proteins · 2021Article
Corrections and comments
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Authors and funding
10 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Vaccinia virus (VACV), the prototype member of the Poxviridae, replicates in the cytoplasm of an infected cell. The catalytic subunit of the DNA polymerase E9 binds the heterodimeric processivity factor A20/D4 to form the functional polymerase holoenzyme. Here we present the crystal structure of full-length E9 at 2.7 Å resolution that permits identification of important poxvirus-specific structural insertions. One insertion in the palm domain interacts with C-terminal residues of A20 and thus serves as the processivity factor-binding site. This is in strong contrast to all other family B polymerases that bind their co-factors at the C terminus of the thumb domain. The VACV E9 structure also permits rationalization of polymerase inhibitor resistance mutations when compared with the closely related eukaryotic polymerase delta-DNA complex.
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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.