Evidence map›Paper›PMID 23022727›Full record

ArticleNature structural & molecular biology2012

Structure of a topoisomerase II-DNA-nucleotide complex reveals a new control mechanism for ATPase activity.

Bryan H Schmidt, Neil Osheroff, James M Berger

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

93 citing papers in PubMed, 159 citations in OpenAlex.

  1. Article
  2. Review
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  6. Review
  7. Structural basis of chiral wrap and T-segment capture byProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
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  10. Article
  11. Article
  12. Article
  13. Article
  14. Circumvention of Topoisomerase IIMolecular pharmacology · 2024
    Article
  15. Article
  16. Article
  17. Structural basis of DNA crossover capture byScience (New York, N.Y.) · 2024
    Article
  18. Article
  19. Article
  20. Article

33 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 at 2 institutions in 1 country.

Bryan H SchmidtDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California, USA.
Neil Osheroff
James M Berger
University of California, Berkeley · USVanderbilt University · US

Funding

MOLECULAR BIOPHYSICS TRAINING GRANTT32GM008295 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HURLEY, JAMES H, WEMMER, DAVID E · 1989 to 2022
$8.1M
Structural and Biochemical Analyses of Type II DNA TopoisomerasesR01CA077373 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERGER, JAMES M. · 1999 to 2021
$7.6M
FUNCTION AND BIOLOGY OF EUKARYOTIC DNA TOPOISOMERASESR01GM033944 · NIGMS · VANDERBILT UNIVERSITY · PI OSHEROFF, NEIL · 1985 to 2015
$5.5M
NCI NIH HHS CA077373NCI NIH HHS R01 CA077373NIGMS NIH HHS GM08295NIGMS NIH HHS GM33944NIGMS NIH HHS R01 GM033944NIGMS NIH HHS T32 GM008295
6 · The paper itself

Abstract

Type IIA topoisomerases control DNA supercoiling and disentangle chromosomes through a complex ATP-dependent strand-passage mechanism. Although a general framework exists for type IIA topoisomerase function, the architecture of the full-length enzyme has remained undefined. Here we present the structure of a fully catalytic Saccharomyces cerevisiae topoisomerase II homodimer complexed with DNA and a nonhydrolyzable ATP analog. The enzyme adopts a domain-swapped configuration wherein the ATPase domain of one protomer sits atop the nucleolytic region of its partner subunit. This organization produces an unexpected interaction between bound DNA and a conformational transducing element in the ATPase domain, which we show is critical for both DNA-stimulated ATP hydrolysis and global topoisomerase activity. Our data indicate that the ATPase domains pivot about each other to ensure unidirectional strand passage and that this state senses bound DNA to promote ATP turnover and enzyme reset.

Indexed as

Models, MolecularProtein ConformationAdenylyl ImidodiphosphateAmino Acid SequenceAntigens, NeoplasmChromatography, GelCrystallizationDimerizationDNADNA-Binding ProteinsDNA Topoisomerases, Type IIMolecular Sequence DataMultiprotein ComplexesSaccharomyces cerevisiaeAdenylyl ImidodiphosphateAntigens, NeoplasmDNADNA-Binding ProteinsDNA Topoisomerases, Type IIMultiprotein Complexes

Identifiers

PMID23022727
PMCPMC3492516
OpenAlexW2129418158

What OpenQuestion holds

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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.