Evidence map›Paper›PMID 24492262›Full record

ArticlePLoS biology2014

Segmental helical motions and dynamical asymmetry modulate histidine kinase autophosphorylation.

Ariel E Mechaly, Nathalie Sassoon, Jean-Michel Betton, Pedro M Alzari

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

72 citing papers in PubMed, 122 citations in OpenAlex.

  1. Conformational diversity in poly-HAMP arrays and its implications for signal transduction.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. A Designed ZnJournal of the American Chemical Society · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Structural insights into redox signal transduction mechanisms in the control of nitrogen fixation by the NifLA system.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  12. Mode of autophosphorylation in bacteriophytochromes RpBphP2 and RpBphP3.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
  13. Article
  14. Experimental Evolution of Copper Resistance inAntibiotics (Basel, Switzerland) · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Sensor Domain of Histidine Kinase VxrA ofJournal of bacteriology · 2021
    Article
  20. Review

12 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Ariel E MechalyInstitut Pasteur, Unité de Microbiologie Structurale and CNRS UMR 3528, Paris, France.
Nathalie SassoonInstitut Pasteur, Unité de Microbiologie Structurale and CNRS UMR 3528, Paris, France.
Jean-Michel BettonInstitut Pasteur, Unité de Microbiologie Structurale and CNRS UMR 3528, Paris, France.
Pedro M AlzariInstitut Pasteur, Unité de Microbiologie Structurale and CNRS UMR 3528, Paris, France.
Institut Pasteur · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histidine kinases (HKs) are dimeric receptors that participate in most adaptive responses to environmental changes in prokaryotes. Although it is well established that stimulus perception triggers autophosphorylation in many HKs, little is known on how the input signal propagates through the HAMP domain to control the transient interaction between the histidine-containing and ATP-binding domains during the catalytic reaction. Here we report crystal structures of the full cytoplasmic region of CpxA, a prototypical HK involved in Escherichia coli response to envelope stress. The structural ensemble, which includes the Michaelis complex, unveils HK activation as a highly dynamic process, in which HAMP modulates the segmental mobility of the central HK α-helices to promote a strong conformational and dynamical asymmetry that characterizes the kinase-active state. A mechanical model based on our structural and biochemical data provides insights into HAMP-mediated signal transduction, the autophosphorylation reaction mechanism, and the symmetry-dependent control of HK kinase/phosphatase functional states.

Indexed as

Models, MolecularAdenosine TriphosphateCatalytic DomainEscherichia coliEscherichia coli ProteinsGene ExpressionHistidineKineticsMotionPhosphorylationProtein BindingProtein KinasesProtein Structure, SecondaryProtein Structure, TertiaryScattering, Small AngleThermodynamicsAdenosine TriphosphateCpxA protein, E coliEscherichia coli ProteinsHistidineProtein Kinases

Identifiers

PMID24492262
PMCPMC3904827
OpenAlexW1966360786

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.