Evidence map›Paper›PMID 27050128›Full record

ArticleActa crystallographica. Section D, Structural biology2016

Structure of a quinolone-stabilized cleavage complex of topoisomerase IV from Klebsiella pneumoniae and comparison with a related Streptococcus pneumoniae complex.

Dennis A Veselkov, Ivan Laponogov, Xiao-Su Pan, Jogitha Selvarajah, Galyna B Skamrova, Arthur Branstrom, Jana Narasimhan, Josyula V N Vara Prasad, L Mark Fisher, Mark R Sanderson

Open access · hybridAbstract readComparative Study
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
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  5. Structural Mechanisms of Topoisomerase-Targeting Drugs.Annual review of biochemistry · 2025
    Review
  6. Review
  7. Article
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  11. Article
  12. Review
  13. Article
  14. Article
  15. Topoisomerases as anticancer targets.The Biochemical journal · 2018
    Review
  16. Article
  17. 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

10 authors at 3 institutions in 2 countries.

Dennis A VeselkovRandall Division of Cell and Molecular Biophysics, King's College London, 3rd Floor, New Hunt's House, Guy's Campus, London SE1 1UL, England.
Ivan LaponogovRandall Division of Cell and Molecular Biophysics, King's College London, 3rd Floor, New Hunt's House, Guy's Campus, London SE1 1UL, England.
Xiao-Su PanCardiovascular and Cell Sciences Research Institute, St George's, University of London, Cranmer Terrace, London SW17 0RE, England.
Jogitha SelvarajahCardiovascular and Cell Sciences Research Institute, St George's, University of London, Cranmer Terrace, London SW17 0RE, England.
Galyna B SkamrovaRandall Division of Cell and Molecular Biophysics, King's College London, 3rd Floor, New Hunt's House, Guy's Campus, London SE1 1UL, England.
Arthur BranstromPTC Therapeutics Inc., 100 Corporate Court, South Plainfield, NJ 07080, USA.
Jana NarasimhanPTC Therapeutics Inc., 100 Corporate Court, South Plainfield, NJ 07080, USA.
Josyula V N Vara PrasadPTC Therapeutics Inc., 100 Corporate Court, South Plainfield, NJ 07080, USA.
L Mark FisherCardiovascular and Cell Sciences Research Institute, St George's, University of London, Cranmer Terrace, London SW17 0RE, England.
Mark R SandersonRandall Division of Cell and Molecular Biophysics, King's College London, 3rd Floor, New Hunt's House, Guy's Campus, London SE1 1UL, England.
St George's, University of London · GBKing's College London · GBPTC Therapeutics (United States) · US

Funding

Biotechnology and Biological Sciences Research Council BB/H00405X/1Biotechnology and Biological Sciences Research Council BB/K10069/1Wellcome Trust
6 · The paper itself

Abstract

Klebsiella pneumoniae is a Gram-negative bacterium that is responsible for a range of common infections, including pulmonary pneumonia, bloodstream infections and meningitis. Certain strains of Klebsiella have become highly resistant to antibiotics. Despite the vast amount of research carried out on this class of bacteria, the molecular structure of its topoisomerase IV, a type II topoisomerase essential for catalysing chromosomal segregation, had remained unknown. In this paper, the structure of its DNA-cleavage complex is reported at 3.35 Å resolution. The complex is comprised of ParC breakage-reunion and ParE TOPRIM domains of K. pneumoniae topoisomerase IV with DNA stabilized by levofloxacin, a broad-spectrum fluoroquinolone antimicrobial agent. This complex is compared with a similar complex from Streptococcus pneumoniae, which has recently been solved.

Indexed as

Bacterial ProteinsDNA, BacterialDNA Topoisomerase IVKlebsiella pneumoniaeQuinolonesStreptococcus pneumoniaeBacterial ProteinsDNA, BacterialDNA Topoisomerase IVQuinolonescleavage complexDNA bindingGram-negative complexesisomeraseisomerase–DNA complexKlebsiella pneumoniaelevofloxacinprotein–DNA–drug complexesquinolonetopoisomerase IVtopoisomerasesX-ray crystallography

Identifiers

PMID27050128
PMCPMC4822561
OpenAlexW2320456355

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.