Evidence map›Paper›PMID 15304566›Full record

ArticleNucleic acids research2004

Structural analysis of the bipartite DNA-binding domain of Tc3 transposase bound to transposon DNA.

Stephan Watkins, Gertie van Pouderoyen, Titia K Sixma

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.7field-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

31 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Jumping Ahead withViruses · 2021
    Review
  3. Article
  4. Article
  5. Article
  6. NMR solution structure of the RED subdomain of the Sleeping Beauty transposase.Protein science : a publication of the Protein Society · 2017
    Article
  7. DNA Transposition at Work.Chemical reviews · 2016
    Review
  8. Crystallization of and selenomethionine phasing strategy for a SETMAR-DNA complex.Acta crystallographica. Section F, Structural biology communications · 2016
    Article
  9. Article
  10. Mechanisms of DNA Transposition.Microbiology spectrum · 2015
    Review
  11. Article
  12. NMR structural analysis of Sleeping Beauty transposase binding to DNA.Protein science : a publication of the Protein Society · 2014
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. DDE transposases: Structural similarity and diversity.Advanced drug delivery reviews · 2010
    Review
  18. Review
  19. Integrating prokaryotes and eukaryotes: DNA transposases in light of structure.Critical reviews in biochemistry and molecular biology · 2010
    Review
  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

3 authors at 1 institution in 1 country.

Stephan WatkinsDivision of Molecular Carcinogenesis, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
Gertie van Pouderoyen
Titia K Sixma
The Netherlands Cancer Institute · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The bipartite DNA-binding domain of Tc3 transposase, Tc3A, was crystallized in complex with its transposon recognition sequence. In the structure the two DNA-binding domains form structurally related helix-turn-helix (HTH) motifs. They both bind to the major groove on a single DNA oligomer, separated by a linker that interacts closely with the minor groove. The structure resembles that of the transcription factor Pax6 DNA-binding domain, but the relative orientation of the HTH-domain is different. The DNA conformation is distorted, characterized by local narrowing of the minor groove and bends at both ends. The protein-DNA recognition takes place through base and backbone contacts, as well as shape-recognition of the distortions in the DNA. Charged interactions are primarily found in the N-terminal domain and the linker indicating that these may form the initial contact area. Two independent dimer interfaces could be relevant for bringing together transposon ends and for binding to a direct repeat site in the transposon end. In contrast to the Tn5 synaptic complex, the two Tc3A DNA-binding domains bind to a single Tc3 transposon end.

Indexed as

DNA Transposable ElementsBase SequenceBinding SitesDimerizationDNADNA-Binding ProteinsModels, MolecularMolecular Sequence DataProtein Structure, TertiaryTransposasesDNADNA-Binding ProteinsDNA Transposable ElementsTransposases

Identifiers

PMID15304566
PMCPMC514390
OpenAlexW2168730873

What OpenQuestion holds

Textmetadata
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.