Evidence map›Paper›PMID 23275567›Full record

ArticleNucleic acids research2013

Crystal structure of an intermediate of rotating dimers within the synaptic tetramer of the G-segment invertase.

Christopher J Ritacco, Satwik Kamtekar, Jimin Wang, Thomas A Steitz

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Snapshots of a molecular swivel in action.Nucleic acids research · 2018
    Article
  10. Article
  11. Article
  12. Article
  13. Serine Resolvases.Microbiology spectrum · 2015
    Review
  14. Article
  15. Article
  16. Exploiting subtle structural differences in heavy-atom derivatives for experimental phasing.Acta crystallographica. Section D, Biological crystallography · 2014
    Article
  17. Article
  18. Article
  19. The ins and outs of serine integrase site-specific recombination.Current opinion in structural biology · 2014
    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

4 authors at 1 institution in 1 country.

Christopher J RitaccoDepartment of Molecular Biophysics and Biochemistry, Department of Chemistry and Howard Hughes Medical Institute, Yale University, New Haven, CT 06520, USA.
Satwik Kamtekar
Jimin Wang
Thomas A Steitz
Howard Hughes Medical Institute · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
STRUCTURES OF DNA POLYMERASES AND FUNCTIONAL COMPLEXESR01GM057510 · NIGMS · YALE UNIVERSITY · PI STEITZ, THOMAS ARTHUR · 1998 to 2013
$4.5M
NIGMS NIH HHS GM057510NIGMS NIH HHS R01 GM057510NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

The serine family of site-specific DNA recombination enzymes accomplishes strand cleavage, exchange and religation using a synaptic protein tetramer. A double-strand break intermediate in which each protein subunit is covalently linked to the target DNA substrate ensures that the recombination event will not damage the DNA. The previous structure of a tetrameric synaptic complex of γδ resolvase linked to two cleaved DNA strands had suggested a rotational mechanism of recombination in which one dimer rotates 180° about the flat exchange interface for strand exchange. Here, we report the crystal structure of a synaptic tetramer of an unliganded activated mutant (M114V) of the G-segment invertase (Gin) in which one dimer half is rotated by 26° or 154° relative to the other dimer when compared with the dimers in the synaptic complex of γδ resolvase. Modeling shows that this rotational orientation of Gin is not compatible with its being able to bind uncleaved DNA, implying that this structure represents an intermediate in the process of strand exchange. Thus, our structure provides direct evidence for the proposed rotational mechanism of site-specific recombination.

Indexed as

Crystallography, X-RayDimerizationDNA NucleotidyltransferasesModels, MolecularProtein ConformationProtein SubunitsDNA invertase GinDNA NucleotidyltransferasesProtein Subunits

Identifiers

PMID23275567
PMCPMC3575834
OpenAlexW2067386691

What OpenQuestion holds

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LicenceCC BY-NC
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.