Evidence map›Paper›PMID 27273516›Full record

ArticleNature structural & molecular biology2016

Direct observation of DNA threading in flap endonuclease complexes.

Faizah A AlMalki, Claudia S Flemming, Jing Zhang, Min Feng, Svetlana E Sedelnikova, Tom Ceska, John B Rafferty, Jon R Sayers, Peter J Artymiuk

Open access · bronzeAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

29 citing papers in PubMed, 41 citations in OpenAlex.

  1. DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026
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  3. Biomolecular NMR assignments · 2025
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  7. Nucleic Acids and Electrical Signals.Reviews of physiology, biochemistry and pharmacology · 2025
    Review
  8. Article
  9. A four-point molecular handover during Okazaki maturation.Nature structural & molecular biology · 2023
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

9 authors at 2 institutions in 1 country.

Faizah A AlMalkiDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.
Claudia S FlemmingDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.
Jing ZhangDepartment of Infection, Immunity &Cardiovascular Disease, University of Sheffield, Sheffield, UK.
Min FengDepartment of Infection, Immunity &Cardiovascular Disease, University of Sheffield, Sheffield, UK.
Svetlana E SedelnikovaDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.
Tom CeskaUCB Pharma, Slough, UK.
John B RaffertyDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.
Jon R SayersDepartment of Infection, Immunity &Cardiovascular Disease, University of Sheffield, Sheffield, UK.ORCID 0000-0002-5082-1443
Peter J ArtymiukDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, UK.
University of Sheffield · GBUCB Pharma (United Kingdom) · GB

Funding

Biotechnology and Biological Sciences Research Council B19466Biotechnology and Biological Sciences Research Council REI18458Medical Research Council MC_PC_13076
6 · The paper itself

Abstract

Maintenance of genome integrity requires that branched nucleic acid molecules be accurately processed to produce double-helical DNA. Flap endonucleases are essential enzymes that trim such branched molecules generated by Okazaki-fragment synthesis during replication. Here, we report crystal structures of bacteriophage T5 flap endonuclease in complexes with intact DNA substrates and products, at resolutions of 1.9-2.2 Å. They reveal single-stranded DNA threading through a hole in the enzyme, which is enclosed by an inverted V-shaped helical arch straddling the active site. Residues lining the hole induce an unusual barb-like conformation in the DNA substrate, thereby juxtaposing the scissile phosphate and essential catalytic metal ions. A series of complexes and biochemical analyses show how the substrate's single-stranded branch approaches, threads through and finally emerges on the far side of the enzyme. Our studies suggest that substrate recognition involves an unusual 'fly-casting, thread, bend and barb' mechanism.

Indexed as

Catalytic DomainCloning, MolecularCrystallography, X-RayDNA, Single-StrandedDNA, ViralEscherichia coliExodeoxyribonucleasesGene ExpressionHydrogen BondingModels, MolecularMutagenesis, Site-DirectedOligonucleotidesProtein BindingProtein Structure, SecondaryRecombinant ProteinsSiphoviridaeDNA, Single-StrandedDNA, ViralExodeoxyribonucleasesOligonucleotidesRecombinant ProteinsT5 D15 exonucleaseViral Proteins

Identifiers

PMID27273516
PMCPMC4939078
OpenAlexW2395799624

What OpenQuestion holds

Textmetadata
LicenceTDM
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.