Evidence map›Paper›PMID 31082213›Full record

ArticleBiochemistry2019

A Noncanonical Chromophore Reveals Structural Rearrangements of the Light-Oxygen-Voltage Domain upon Photoactivation.

Mindaugas E Kalvaitis, Luke A Johnson, Robert J Mart, Pierre Rizkallah, Rudolf K Allemann

Open access · hybridAbstract read
In one paragraph

Article in Biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Extreme dependence of Chloroflexus aggregans LOV domain thermo- and photostability on the bound flavin species.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Signal transduction in photoreceptor histidine kinases.Protein science : a publication of the Protein Society · 2019
    Review
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 at 2 institutions in 1 country.

Mindaugas E KalvaitisSchool of Chemistry , Cardiff University , Park Place , Cardiff CF10 3AT , United Kingdom.ORCID 0000-0002-8175-7552
Luke A JohnsonSchool of Chemistry , Cardiff University , Park Place , Cardiff CF10 3AT , United Kingdom.ORCID 0000-0002-6697-6589
Robert J MartSchool of Chemistry , Cardiff University , Park Place , Cardiff CF10 3AT , United Kingdom.ORCID 0000-0003-2196-5840
Pierre RizkallahSchool of Medicine , University Hospital Wales , Main Building, Heath Park , Cardiff CF14 4XN , United Kingdom.ORCID 0000-0002-9290-0369
Rudolf K AllemannSchool of Chemistry , Cardiff University , Park Place , Cardiff CF10 3AT , United Kingdom.ORCID 0000-0002-1323-8830
Cardiff University · GBUniversity Hospital of Wales · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M006158/1Biotechnology and Biological Sciences Research Council BB/P009980/1
6 · The paper itself

Abstract

Light-oxygen-voltage (LOV) domains are increasingly used to engineer photoresponsive biological systems. While the photochemical cycle is well documented, the allosteric mechanism by which formation of a cysteinyl-flavin adduct leads to activation is unclear. Via replacement of flavin mononucleotide (FMN) with 5-deazaflavin mononucleotide (5dFMN) in the Aureochrome1a (Au1a) transcription factor from Ochromonas danica, a thermally stable cysteinyl-5dFMN adduct was generated. High-resolution crystal structures (<2 Å) under different illumination conditions with either FMN or 5dFMN chromophores reveal three conformations of the highly conserved glutamine 293. An allosteric hydrogen bond network linking the chromophore via Gln293 to the auxiliary A'α helix is observed. With FMN, a "flip" of the Gln293 side chain occurs between dark and lit states. 5dFMN cannot hydrogen bond through the C5 position and proved to be unable to support Au1a domain dimerization. Under blue light, the Gln293 side chain instead "swings" away in a conformation distal to the chromophore and not previously observed in existing LOV domain structures. Together, the multiple side chain conformations of Gln293 and functional analysis of 5dFMN provide new insight into the structural requirements for LOV domain activation.

Indexed as

Algal ProteinsCysteineFlavin MononucleotideFlavinsGlutamineLightOchromonasProtein ConformationProtein DomainsRibonucleotidesTranscription Factors5-deazaflavinAlgal ProteinsCysteineFlavin MononucleotideFlavinsGlutamineRibonucleotidesTranscription Factors

Identifiers

PMID31082213
PMCPMC7007005
OpenAlexW2946158781

What OpenQuestion holds

Textmetadata
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.