Evidence map›Paper›PMID 24174528›Full record

ArticleThe Journal of biological chemistry2013

Structure of the cyanobacterial phytochrome 2 photosensor implies a tryptophan switch for phytochrome signaling.

Katrin Anders, Grazia Daminelli-Widany, Maria Andrea Mroginski, David von Stetten, Lars-Oliver Essen

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing 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

57 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025
    Review
  7. Article
  8. Article
  9. Article
  10. Responding to light signals: a comprehensive update on photomorphogenesis in cyanobacteria.Physiology and molecular biology of plants : an international journal of functional plant biology · 2023
    Review
  11. Article
  12. Evidence for an early green/red photocycle that precedes the diversification of GAF domain photoreceptor cyanobacteriochromes.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2023
    Article
  13. Influence of the PHY domain on the ms-photoconversion dynamics of a knotless phytochrome.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Ultrafast Photoconversion Dynamics of the Knotless PhytochromeInternational journal of molecular sciences · 2021
    Article
  19. Phytochrome Signaling Networks.Annual review of plant biology · 2021
    Review
  20. 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

5 authors.

Katrin AndersFrom the Department of Chemistry, Biomedical Research Centre, Philipps-Universität, D-35032 Marburg, Germany.
Grazia Daminelli-Widany
Maria Andrea Mroginski
David von Stetten
Lars-Oliver Essen

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phytochromes are highly versatile photoreceptors, which occur ubiquitously in plants as well as in many light-responsive microorganisms. Here, photosynthetic cyanobacteria utilize up to three different phytochrome architectures, where only the plant-like and the single-domain cyanobacteriochromes are structurally characterized so far. Cph2 represents a third group in Synechocystis species and affects their capability of phototaxis by controlling c-di-GMP synthesis and degradation. The 2.6-Å crystal structure of its red/far-red responsive photosensory module in the Pr state reveals a tandem-GAF bidomain that lacks the figure-of-eight knot of the plant/cph1 subfamily. Its covalently attached phycocyanobilin chromophore adopts a highly tilted ZZZssa conformation with a novel set of interactions between its propionates and the GAF1 domain. The tongue-like protrusion from the GAF2 domain interacts with the GAF1-bound chromophore via its conserved PRXSF, WXE, and W(G/A)G motifs. Mutagenesis showed that the integrity of the tongue is indispensable for Pr → Pfr photoconversion and involves a swap of the motifs' tryptophans within the tongue-GAF1 interface. This "Trp switch" is supposed to be a crucial element for the photochromicity of all multidomain phytochromes.

Indexed as

Signal TransductionTryptophanAmino Acid MotifsAmino Acid SequenceBacterial ProteinsBinding SitesCrystallography, X-RayModels, MolecularMolecular Sequence DataPhotosynthesisPhycobilinsPhycocyaninPhytochromeProtein Structure, TertiarySynechocystisBacterial ProteinsCph2 protein, bacteriaPhycobilinsPhycocyaninphycocyanobilinPhytochromeTryptophanBiliproteinc-di-GMP SignalingCyanobacteriaPhotochromicityPhytochromeProtein ConformationRed Light PhotoreceptorSignalingSignal TransductionStructural Biology

Identifiers

PMID24174528
PMCPMC3861623

What OpenQuestion holds

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Registered trials

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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.