ArticleJournal of molecular biology2007
Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
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Who cites it
106 citing papers in PubMed, 235 citations in OpenAlex.
- Sequential structural changes in the monomeric LOV histidine kinase EL346 revealed by transient infrared spectroscopy.Physical chemistry chemical physics : PCCP · 2026Article
- Dimer asymmetry in signaling of blue light sensor histidine kinases.Science advances · 2026Article
- Conserved structural motifs in PAS, LOV, and CRY proteins regulate circadian rhythms and are therapeutic targets.FEBS letters · 2026Review
- Archaeal LOV domains from Lake Diamante: first functional characterization of a halo-adapted photoreceptor.Frontiers in microbiology · 2025Article
- Article
- Structural dynamics of protein-protein association involved in the light-induced transition of Avena sativa LOV2 protein.Nature communications · 2024Article
- Light Control in Microbial Systems.International journal of molecular sciences · 2024Review
- Recent advances in bioluminescent probes for neurobiology.Neurophotonics · 2024Article
- Elucidating the Signal Transduction Mechanism of the Blue-Light-Regulated Photoreceptor YtvA: From Photoactivation to Downstream Regulation.ACS chemical biology · 2024Article
- From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons.Acta crystallographica. Section D, Structural biology · 2024Article
- Gas and light: triggers of c-di-GMP-mediated regulation.FEMS microbiology reviews · 2023Review
- LOV2-based photoactivatable CaMKII and its application to single synapses: Local Optogenetics.Biophysics and physicobiology · 2023Article
- Optophysiology: Illuminating cell physiology with optogenetics.Physiological reviews · 2022Review
- Signal transduction in light-oxygen-voltage receptors lacking the active-site glutamine.Nature communications · 2022Article
- Phylogenetic Analysis with Prediction of Cofactor or Ligand Binding for Pseudomonas aeruginosa PAS and Cache Domains.Microbiology spectrum · 2021Article
- Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021Review
- Bioluminescence and Photoreception in Unicellular Organisms: Light-Signalling in a Bio-Communication Perspective.International journal of molecular sciences · 2021Review
- Natural diversity provides a broad spectrum of cyanobacteriochrome-based diguanylate cyclases.Plant physiology · 2021Article
- Dimeric allostery mechanism of the plant circadian clock photoreceptor ZEITLUPE.PLoS computational biology · 2021Article
- Transmission of light signals from the light-oxygen-voltage core via the hydrophobic region of the β-sheet surface in aureochrome-1.Scientific reports · 2021Article
46 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The photosensor YtvA binds flavin mononucleotide and regulates the general stress reaction in Bacillus subtilis in response to blue light illumination. It belongs to the family of light-oxygen-voltage (LOV) proteins that were first described in plant phototropins and form a subgroup of the Per-Arnt-Sim (PAS) superfamily. Here, we report the three-dimensional structure of the LOV domain of YtvA in its dark and light states. The protein assumes the global fold common to all PAS domains and dimerizes via a hydrophobic interface. Directly C-terminal to the core of the LOV domain, an alpha-helix extends into the solvent. Light absorption causes formation of a covalent bond between a conserved cysteine residue and atom C(4a) of the FMN ring, which triggers rearrangements throughout the LOV domain. Concomitantly, in the dark and light structures, the two subunits of the dimeric protein rotate relative to each other by 5 degrees . This small quaternary structural change is presumably a component of the mechanism by which the activity of YtvA is regulated in response to light. In terms of both structure and signaling mechanism, YtvA differs from plant phototropins and more closely resembles prokaryotic heme-binding PAS domains.
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Registered trials
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.