Evidence map›Paper›PMID 27679804›Full record

ArticleStructural dynamics (Melville, N.Y.)2016

Light-induced structural changes in a monomeric bacteriophytochrome.

Heikki Takala, Stephan Niebling, Oskar Berntsson, Alexander Björling, Heli Lehtivuori, Heikki Häkkänen, Matthijs Panman, Emil Gustavsson, Maria Hoernke, Gemma Newby and 5 more

Open access · goldAbstract read
In one paragraph

Article in Structural dynamics (Melville, N.Y.), 2016. 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
9.6field-weighted citation impact, top 3% 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

19 citing papers in PubMed, 46 citations in OpenAlex.

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  6. The structural effect between the output module and chromophore-binding domain is a two-way street via the hairpin extension.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Article
  7. Vibrational couplings between protein and cofactor in bacterial phytochrome Agp1 revealed by 2D-IR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

15 authors at 5 institutions in 5 countries.

Heikki Takala
Stephan NieblingDepartment of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
Oskar BerntssonDepartment of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
Alexander BjörlingDepartment of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
Heli Lehtivuori
Heikki HäkkänenNanoscience Center, Department of Biological and Environmental Sciences, University of Jyvaskyla , Jyväskylä 40014, Finland.
Matthijs PanmanDepartment of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
Emil GustavssonDepartment of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
Maria Hoernke
Gemma NewbyESRF-The European Synchrotron Radiation Facility , CS40220, 38043 Grenoble Cedex 9, France.
Federico ZontoneESRF-The European Synchrotron Radiation Facility , CS40220, 38043 Grenoble Cedex 9, France.
Michael WulffESRF-The European Synchrotron Radiation Facility , CS40220, 38043 Grenoble Cedex 9, France.
Andreas MenzelPaul Scherrer Institut , 5232 Villigen PSI, Switzerland.
Janne A IhalainenNanoscience Center, Department of Biological and Environmental Sciences, University of Jyvaskyla , Jyväskylä 40014, Finland.
Sebastian WestenhoffDepartment of Chemistry and Molecular Biology, University of Gothenburg , Gothenburg 40530, Sweden.
Paul Scherrer Institute · CHUniversity of Gothenburg · SEUniversity of Helsinki · FIEuropean Synchrotron Radiation Facility · FRUniversity of Freiburg · DE

Funding

European Research Council 279944
6 · The paper itself

Abstract

Phytochromes sense red light in plants and various microorganism. Light absorption causes structural changes within the protein, which alter its biochemical activity. Bacterial phytochromes are dimeric proteins, but the functional relevance of this arrangement remains unclear. Here, we use time-resolved X-ray scattering to reveal the solution structural change of a monomeric variant of the photosensory core module of the phytochrome from Deinococcus radiodurans. The data reveal two motions, a bend and a twist of the PHY domain with respect to the chromophore-binding domains. Infrared spectroscopy shows the refolding of the PHY tongue. We conclude that a monomer of the phytochrome photosensory core is sufficient to perform the light-induced structural changes. This implies that allosteric cooperation with the other monomer is not needed for structural activation. The dimeric arrangement may instead be intrinsic to the biochemical output domains of bacterial phytochromes.

Identifiers

PMID27679804
PMCPMC5010554
OpenAlexW2512376910

What OpenQuestion holds

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LicenceCC BY
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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.