Evidence map›Paper›PMID 21645851›Full record

ArticleStructure (London, England : 1993)2011

Structural basis for catalytic activation of a serine recombinase.

Ross A Keenholtz, Sally-J Rowland, Martin R Boocock, W Marshall Stark, Phoebe A Rice

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Staphylococcal Cassette ChromosomeAntibiotics (Basel, Switzerland) · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Snapshots of a molecular swivel in action.Nucleic acids research · 2018
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Serine Resolvases.Microbiology spectrum · 2015
    Review
  14. Mechanisms of DNA Transposition.Microbiology spectrum · 2015
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. The ins and outs of serine integrase site-specific recombination.Current opinion in structural biology · 2014
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Ross A KeenholtzDepartment of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637, USA.
Sally-J Rowland
Martin R Boocock
W Marshall Stark
Phoebe A Rice

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Mechanisms and regulation of serine resolvasesR01GM086826 · NIGMS · UNIVERSITY OF CHICAGO · PI RICE, PHOEBE A · 2009 to 2012
$1.3M
NIGMS NIH HHS 5T32GM007183-35NIGMS NIH HHS R01 GM086826NIGMS NIH HHS R01-GM086826NIGMS NIH HHS T32 GM007183Wellcome TrustWellcome Trust 072552
6 · The paper itself

Abstract

Sin resolvase is a site-specific serine recombinase that is normally controlled by a complex regulatory mechanism. A single mutation, Q115R, allows the enzyme to bypass the entire regulatory apparatus, such that no accessory proteins or DNA sites are required. Here, we present a 1.86 Å crystal structure of the Sin Q115R catalytic domain, in a tetrameric arrangement stabilized by an interaction between Arg115 residues on neighboring subunits. The subunits have undergone significant conformational changes from the inactive dimeric state previously reported. The structure provides a new high-resolution view of a serine recombinase active site that is apparently fully assembled, suggesting roles for the conserved active site residues. The structure also suggests how the dimer-tetramer transition is coupled to assembly of the active site. The tetramer is captured in a different rotational substate than that seen in previous hyperactive serine recombinase structures, and unbroken crossover site DNA can be readily modeled into its active sites.

Indexed as

Bacterial ProteinsCatalytic DomainComputer SimulationCrystallography, X-RayDNA NucleotidyltransferasesEnzyme ActivationHydrogen BondingHydrophobic and Hydrophilic InteractionsModels, MolecularMutation, MissenseNucleic Acid ConformationOligonucleotidesProtein BindingProtein Structure, QuaternaryProtein Structure, SecondaryStaphylococcus aureusBacterial ProteinsDNA NucleotidyltransferasesOligonucleotidessin protein, Staphylococcus aureus

Identifiers

PMID21645851
PMCPMC3238390

What OpenQuestion holds

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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.