Evidence map›Paper›PMID 16107542›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Structure of a bacterial BLUF photoreceptor: insights into blue light-mediated signal transduction.

Astrid Jung, Tatiana Domratcheva, Marina Tarutina, Qiong Wu, Wen-Huang Ko, Robert L Shoeman, Mark Gomelsky, Kevin H Gardner, Ilme Schlichting

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
17.4field-weighted citation impact, top 1% 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

64 citing papers in PubMed, 174 citations in OpenAlex.

  1. Antimicrobial blue light inactivatesFood chemistry: X · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Optogenetics at the presynapse.Nature neuroscience · 2022
    Review
  12. Time-resolved diffusion reveals photoreactions of BLUF proteins with similar functional domains.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022
    Review
  13. Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021
    Review
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

4 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

9 authors at 3 institutions in 2 countries.

Astrid JungMax Planck Institute for Medical Research, Department of Biomolecular Mechanisms, Jahnstrasse 29, 69120 Heidelberg, Germany.
Tatiana Domratcheva
Marina Tarutina
Qiong Wu
Wen-Huang Ko
Robert L Shoeman
Mark Gomelsky
Kevin H Gardner
Ilme Schlichting
Max Planck Institute for Medical Research · DEUniversity of Wyoming · USThe University of Texas Southwestern Medical Center · US

Funding

VENTRICULAR MYOCYTE FUNCTION IN HEALTH AND DISEASEP20RR015640 · NCRR · UNIVERSITY OF WYOMING · PI SKINNER, DONAL C · 2000 to 2010
$15.7M
NCRR NIH HHS P20 RR015640NCRR NIH HHS P20 RR15640
6 · The paper itself

Abstract

Light is an essential environmental factor, and many species have evolved the capability to respond to it. Blue light is perceived through three flavin-containing photoreceptor families: cryptochromes, light-oxygen-voltage, and BLUF (sensor of blue light using flavin adenine dinucleotide, FAD) domain proteins. BLUF domains are present in various proteins from Bacteria and lower Eukarya. They are fully modular and can relay signals to structurally and functionally diverse output units, most of which are implicated in nucleotide metabolism. We present the high resolution crystal structure of the dark resting state of BlrB, a short BLUF domain-containing protein from Rhodobacter sphaeroides. The structure reveals a previously uncharacterized FAD-binding fold. Along with other lines of evidence, it suggests mechanistic aspects for the photocycle that is characterized by a red-shifted absorbance of the flavin. The isoalloxazine ring of FAD binds in a cleft between two helices, whereas the adenine ring points into the solvent. We propose that the adenine ring serves as a hook mediating the interaction with its effector/output domain. The structure suggests a unique photochemical signaling switch in which the absorption of light induces a structural change in the rim surrounding the hook, thereby changing the protein interface between BLUF and the output domain.

Indexed as

Bacterial ProteinsBinding SitesCrystallography, X-RayFlavin-Adenine DinucleotideLightModels, BiologicalModels, MolecularPhotochemistryPhotoreceptors, MicrobialProtein Structure, TertiaryRecombinant ProteinsRhodobacter sphaeroidesSignal TransductionSpectrophotometryBacterial ProteinsFlavin-Adenine DinucleotidePhotoreceptors, MicrobialRecombinant Proteins

Identifiers

PMID16107542
PMCPMC1194903
OpenAlexW2045013780

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.