Evidence map›Paper›PMID 29968711›Full record

ArticleNature communications2018

Trapping of the transport-segment DNA by the ATPase domains of a type II topoisomerase.

Ivan Laponogov, Xiao-Su Pan, Dennis A Veselkov, Galyna B Skamrova, Trishant R Umrekar, L Mark Fisher, Mark R Sanderson

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Structural basis of chiral wrap and T-segment capture byProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Structural basis of DNA crossover capture byScience (New York, N.Y.) · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. The pentapeptide-repeat protein, MfpA, interacts with mycobacterial DNA gyrase as a DNA T-segment mimic.Proceedings of the National Academy of Sciences of the United States of America · 2021
    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

7 authors at 2 institutions in 1 country.

Ivan LaponogovRandall Centre for Cell and Molecular Biophysics, 3rd Floor New Hunt's House, Faculty of Life Sciences and Medicine, King's College London, London, SE1 1UL, UK.
Xiao-Su PanMolecular and Clinical Sciences Research Institute, St. George's, University of London, Cranmer Terrace, London, SW17 0RE, UK.
Dennis A VeselkovRandall Centre for Cell and Molecular Biophysics, 3rd Floor New Hunt's House, Faculty of Life Sciences and Medicine, King's College London, London, SE1 1UL, UK.
Galyna B SkamrovaRandall Centre for Cell and Molecular Biophysics, 3rd Floor New Hunt's House, Faculty of Life Sciences and Medicine, King's College London, London, SE1 1UL, UK.
Trishant R UmrekarRandall Centre for Cell and Molecular Biophysics, 3rd Floor New Hunt's House, Faculty of Life Sciences and Medicine, King's College London, London, SE1 1UL, UK.ORCID http://orcid.org/0000-0003-3138-4185
L Mark FisherMolecular and Clinical Sciences Research Institute, St. George's, University of London, Cranmer Terrace, London, SW17 0RE, UK. lfisher@sgul.ac.uk.ORCID http://orcid.org/0000-0002-2172-3369
Mark R SandersonRandall Centre for Cell and Molecular Biophysics, 3rd Floor New Hunt's House, Faculty of Life Sciences and Medicine, King's College London, London, SE1 1UL, UK. mark.sanderson@kcl.ac.uk.ORCID http://orcid.org/0000-0003-4235-7780
King's College London · GBSt George's, University of London · GB

Funding

Biotechnology and Biological Sciences Research Council (BBSRC) BB/K010069/1
6 · The paper itself

Abstract

Type II topoisomerases alter DNA topology to control DNA supercoiling and chromosome segregation and are targets of clinically important anti-infective and anticancer therapeutics. They act as ATP-operated clamps to trap a DNA helix and transport it through a transient break in a second DNA. Here, we present the first X-ray crystal structure solved at 2.83 Å of a closed clamp complete with trapped T-segment DNA obtained by co-crystallizing the ATPase domain of S. pneumoniae topoisomerase IV with a nonhydrolyzable ATP analogue and 14-mer duplex DNA. The ATPase dimer forms a 22 Å protein hole occupied by the kinked DNA bound asymmetrically through positively charged residues lining the hole, and whose mutagenesis impacts the DNA decatenation, DNA relaxation and DNA-dependent ATPase activities of topo IV. These results and a side-bound DNA-ParE structure help explain how the T-segment DNA is captured and transported by a type II topoisomerase, and reveal a new enzyme-DNA interface for drug discovery.

Indexed as

Adenosine TriphosphateCrystallography, X-RayDNADNA, BacterialDNA Topoisomerase IVMutagenesis, Site-DirectedProtein DomainsAdenosine TriphosphateDNADNA, BacterialDNA Topoisomerase IVkinked DNAT-DNA

Identifiers

PMID29968711
PMCPMC6030046
OpenAlexW2810279148

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.