Evidence map›Paper›PMID 21035462›Full record

ArticleJournal of molecular biology2011

Crystal structure of the phage T4 recombinase UvsX and its functional interaction with the T4 SF2 helicase UvsW.

Stefan Gajewski, Michael R Webb, Vitold Galkin, Edward H Egelman, Kenneth N Kreuzer, Stephen W White

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

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  13. Structure and mechanism of the phage T4 recombination mediator protein UvsY.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Presynaptic filament dynamics in homologous recombination and DNA repair.Critical reviews in biochemistry and molecular biology · 2011
    Article
  19. Review
  20. Review
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

6 authors at 4 institutions in 2 countries.

Stefan GajewskiDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN 38105, USA.
Michael R Webb
Vitold Galkin
Edward H Egelman
Kenneth N Kreuzer
Stephen W White
Duke Medical Center · USUniversity of Virginia · USUniversity of Graz · ATUniversity of Tennessee Health Science Center · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
STRUCTURAL STUDIES OF RECA FILAMENTSR01GM035269 · NIGMS · YALE UNIVERSITY · PI EGELMAN, EDWARD H. · 1986 to 2016
$5.2M
Recombination and fork progression in bacteriophage T4R01GM066934 · NIGMS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI KREUZER, KENNETH N, WHITE, STEPHEN W · 2004 to 2013
$2.8M
NCI NIH HHS CA21765NCI NIH HHS P30 CA021765NIGMS NIH HHS GM035269NIGMS NIH HHS GM066934NIGMS NIH HHS R01 GM035269NIGMS NIH HHS R01 GM066934
6 · The paper itself

Abstract

Bacteriophage T4 provides an important model system for studying the mechanism of homologous recombination. We have determined the crystal structure of the T4 UvsX recombinase, and the overall architecture and fold closely resemble those of RecA, including a highly conserved ATP binding site. Based on this new structure, we reanalyzed electron microscopy reconstructions of UvsX-DNA filaments and docked the UvsX crystal structure into two different filament forms: a compressed filament generated in the presence of ADP and an elongated filament generated in the presence of ATP and aluminum fluoride. In these reconstructions, the ATP binding site sits at the protomer interface, as in the RecA filament crystal structure. However, the environment of the ATP binding site is altered in the two filament reconstructions, suggesting that nucleotide cannot be as easily accommodated at the protomer interface of the compressed filament. Finally, we show that the phage helicase UvsW completes the UvsX-promoted strand-exchange reaction, allowing the generation of a simple nicked circular product rather than complex networks of partially exchanged substrates.

Indexed as

Amino Acid SequenceBacteriophage T4Crystallography, X-RayDNA-Binding ProteinsDNA HelicasesDNA, ViralMembrane ProteinsModels, MolecularMolecular Sequence DataProtein BindingProtein Interaction MappingProtein Structure, TertiaryRecombination, GeneticViral ProteinsDNA-Binding ProteinsDNA HelicasesDNA, ViralMembrane ProteinsUvsW protein, Bacteriophage T4UvsX protein, Enterobacteria phage T4Viral Proteins

Identifiers

PMID21035462
PMCPMC3006652
OpenAlexW2079396057

What OpenQuestion holds

Textmetadata
LicenceTDM
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.