Evidence map›Paper›PMID 15755748›Full record

ArticleNucleic acids research2005

Conformational flexibility revealed by the crystal structure of a crenarchaeal RadA.

Antonio Ariza, Derek J Richard, Malcolm F White, Charles S Bond

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  3. Review
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  5. Article
  6. Review
  7. Review
  8. Structure of a filament of stacked octamers of human DMC1 recombinase.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  9. Structure of a hexameric form of RadA recombinase from Methanococcus voltae.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  10. Target molecular simulations of RecA family protein filaments.International journal of molecular sciences · 2012
    Article
  11. Article
  12. Article
  13. Article
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  15. Article
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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

4 authors at 1 institution in 1 country.

Antonio ArizaDivision of Biological Chemistry and Molecular Microbiology, School of Life Sciences, University of Dundee Dow St, Dundee, DD1 5EH, UK.
Derek J Richard
Malcolm F White
Charles S Bond
University of Dundee · GB

Funding

Biotechnology and Biological Sciences Research Council C19814
6 · The paper itself

Abstract

Homologous recombinational repair is an essential mechanism for repair of double-strand breaks in DNA. Recombinases of the RecA-fold family play a crucial role in this process, forming filaments that utilize ATP to mediate their interactions with single- and double-stranded DNA. The recombinase molecules present in the archaea (RadA) and eukaryota (Rad51) are more closely related to each other than to their bacterial counterpart (RecA) and, as a result, RadA makes a suitable model for the eukaryotic system. The crystal structure of Sulfolobus solfataricus RadA has been solved to a resolution of 3.2 A in the absence of nucleotide analogues or DNA, revealing a narrow filamentous assembly with three molecules per helical turn. As observed in other RecA-family recombinases, each RadA molecule in the filament is linked to its neighbour via interactions of a short beta-strand with the neighbouring ATPase domain. However, despite apparent flexibility between domains, comparison with other structures indicates conservation of a number of key interactions that introduce rigidity to the system, allowing allosteric control of the filament by interaction with ATP. Additional analysis reveals that the interaction specificity of the five human Rad51 paralogues can be predicted using a simple model based on the RadA structure.

Indexed as

Models, MolecularAmino Acid SequenceArchaeal ProteinsCrystallography, X-RayDNA-Binding ProteinsHumansMolecular Sequence DataProtein ConformationProtein Structure, QuaternaryRad51 RecombinaseSulfolobus solfataricusArchaeal ProteinsDNA-Binding ProteinsRAD51 protein, humanRad51 RecombinaseRadA protein, archaeal

Identifiers

PMID15755748
PMCPMC1062875
OpenAlexW2067746015

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.