Evidence map›Paper›PMID 10411889›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

A model for the mechanism of strand passage by DNA gyrase.

S C Kampranis, A D Bates, A Maxwell

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
–field-weighted citation impact
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

62 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Structural basis of chiral wrap and T-segment capture byProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Rapid Detection of Quinolone Resistance Mutations inPathogens (Basel, Switzerland) · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Topoisomerases as anticancer targets.The Biochemical journal · 2018
    Review
  16. Article
  17. Thiophene antibacterials that allosterically stabilize DNA-cleavage complexes with DNA gyrase.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. DNA Topoisomerases.EcoSal Plus · 2015
    Review
  20. Plasmid-mediated quinolone resistance.Microbiology spectrum · 2014
    Review

2 more citing papers are in PubMed but not listed here.

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

3 authors.

S C KampranisDepartment of Biochemistry, University of Leicester, Leicester LE1 7RH, United Kingdom.
A D Bates
A Maxwell

Funding

Wellcome Trust
6 · The paper itself

Abstract

The mechanism of type II DNA topoisomerases involves the formation of an enzyme-operated gate in one double-stranded DNA segment and the passage of another segment through this gate. DNA gyrase is the only type II topoisomerase able to introduce negative supercoils into DNA, a feature that requires the enzyme to dictate the directionality of strand passage. Although it is known that this is a consequence of the characteristic wrapping of DNA by gyrase, the detailed mechanism by which the transported DNA segment is captured and directed through the DNA gate is largely unknown. We have addressed this mechanism by probing the topology of the bound DNA segment at distinct steps of the catalytic cycle. We propose a model in which gyrase captures a contiguous DNA segment with high probability, irrespective of the superhelical density of the DNA substrate, setting up an equilibrium of the transported segment across the DNA gate. The overall efficiency of strand passage is determined by the position of this equilibrium, which depends on the superhelical density of the DNA substrate. This mechanism is concerted, in that capture of the transported segment by the ATP-operated clamp induces opening of the DNA gate, which in turn stimulates ATP hydrolysis.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateBinding SitesDNADNA, SuperhelicalDNA Topoisomerases, Type IDNA Topoisomerases, Type IIEscherichia coliModels, MolecularMutationNucleic Acid ConformationProtein ConformationAdenosine TriphosphatasesAdenosine TriphosphateDNADNA, SuperhelicalDNA Topoisomerases, Type IDNA Topoisomerases, Type II

Identifiers

PMID10411889
PMCPMC17530

What OpenQuestion holds

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Registered trials

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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.