Evidence map›Paper›PMID 24500202›Full record

ArticleNucleic acids research2014

Structural insights into the dimerization of the response regulator ComE from Streptococcus pneumoniae.

Marion Boudes, Dyana Sanchez, Marc Graille, Herman van Tilbeurgh, Dominique Durand, Sophie Quevillon-Cheruel

Abstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Repurposing Diflunisal as an Antivirulence Agent AgainstInfectious microbes & diseases · 2025
    Article
  3. Competence Regulation inCurrent medicinal chemistry · 2025
    Review
  4. Article
  5. Microbiology spectrum · 2023
    Article
  6. Article
  7. Article
  8. Natural Transformation inFrontiers in microbiology · 2020
    Article
  9. Article
  10. Article
  11. Dynamic Modeling ofFrontiers in microbiology · 2018
    Article
  12. Article
  13. Article
  14. Large-scale identification of coevolution signals across homo-oligomeric protein interfaces by direct coupling analysis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Review
  16. Feedback Control of Two-Component Regulatory Systems.Annual review of microbiology · 2016
    Review
  17. Can I solve my structure by SAD phasing? Anomalous signal in SAD phasing.Acta crystallographica. Section D, Structural biology · 2016
    Article
  18. Article
  19. 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

6 authors.

Marion BoudesInstitut de Biochimie et de Biophysique Moléculaire et Cellulaire, Université de Paris-Sud XI, UMR8619, Bât 430, 91405 Orsay, France and Centre National de la Recherche Scientifique, Orsay, 91405, France.
Dyana Sanchez
Marc Graille
Herman van Tilbeurgh
Dominique Durand
Sophie Quevillon-Cheruel

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural transformation contributes to the maintenance and to the evolution of the bacterial genomes. In Streptococcus pneumoniae, this function is reached by achieving the competence state, which is under the control of the ComD-ComE two-component system. We present the crystal and solution structures of ComE. We mimicked the active and non-active states by using the phosphorylated mimetic ComE(D58E) and the unphosphorylatable ComE(D58A) mutants. In the crystal, full-length ComE(D58A) dimerizes through its canonical REC receiver domain but with an atypical mode, which is also adopted by the isolated REC(D58A) and REC(D58E). The LytTR domain adopts a tandem arrangement consistent with the two direct repeats of its promoters. However ComE(D58A) is monomeric in solution, as seen by SAXS, by contrast to ComE(D58E) that dimerizes. For both, a relative mobility between the two domains is assumed. Based on these results we propose two possible ways for activation of ComE by phosphorylation.

Indexed as

Bacterial ProteinsModels, MolecularPhosphorylationProtein MultimerizationProtein Structure, TertiaryBacterial ProteinsComE protein, Streptococcus pneumoniae

Identifiers

PMID24500202
PMCPMC4005675

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.