ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Coiled-coil dimerization of the LOV2 domain of the blue-light photoreceptor phototropin 1 from Arabidopsis thaliana.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 38 citations in OpenAlex.
- Small Molecule Regulation of CLOCK:BMAL1 DNA Binding Activity.bioRxiv : the preprint server for biology · 2026Article
- Article
- Structural dynamics of protein-protein association involved in the light-induced transition of Avena sativa LOV2 protein.Nature communications · 2024Article
- PAS Dimerization at the Nexus of the Mammalian Circadian Clock.Journal of molecular biology · 2024Review
- Plug-and-Display Photo-Switchable Systems on Plant Virus Nanoparticles.Biotech (Basel (Switzerland)) · 2022Article
- The emergence of molecular systems neuroscience.Molecular brain · 2022Review
- GIpred: a computational tool for prediction of GIGANTEA proteins using machine learning algorithm.Physiology and molecular biology of plants : an international journal of functional plant biology · 2022Article
- 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
- Domain Organization in Plant Blue-Light Receptor Phototropin2 ofInternational journal of molecular sciences · 2020Review
- Millisecond time-resolved serial oscillation crystallography of a blue-light photoreceptor at a synchrotron.IUCrJ · 2020Article
- Engineering the phototropin photocycle improves photoreceptor performance and plant biomass production.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Helical Contributions Mediate Light-Activated Conformational Change in the LOV2 Domain ofACS omega · 2019Article
- Blue-Light Receptors for Optogenetics.Chemical reviews · 2018Review
- Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein.PloS one · 2018Article
- Functional characterization of a constitutively active kinase variant ofThe Journal of biological chemistry · 2017Article
- Blue Light-excited Light-Oxygen-Voltage-sensing Domain 2 (LOV2) Triggers a Rearrangement of the Kinase Domain to Induce Phosphorylation Activity in Arabidopsis Phototropin1.The Journal of biological chemistry · 2016Article
- Molecular mechanism of phototropin light signaling.Journal of plant research · 2016Review
- Plant flavoprotein photoreceptors.Plant & cell physiology · 2015Review
- Light-induced structural changes in a short light, oxygen, voltage (LOV) protein revealed by molecular dynamics simulations-implications for the understanding of LOV photoactivation.Frontiers in molecular biosciences · 2015Article
- Setting the PAS, the role of circadian PAS domain proteins during environmental adaptation in plants.Frontiers in plant science · 2015Review
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2 authors at 1 institution in 1 country.
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Abstract
A key role in signal transduction and dimerization mediated by Per-Arnt-Sim (PAS) domains is played by α-helical linkers that flank the structurally similar α/β cores of these domains. However, crystal-packing forces and the different construct lengths and sequences of the PAS domains influence the final length and orientation of the linkers relative to the core and create uncertainty in the exact mechanism of the linker function. Thus, structural characterization and comparison of the linkers within isolated PAS-domain constructs and/or full-length PAS-containing proteins is important for clarification of the mechanism. The plant blue-light photoreceptors phototropins possess two N-terminal flavin mononucleotide-based light, oxygen or voltage (LOV) domains (LOV1 and LOV2) that comprise a subclass of the PAS family and one C-terminal serine/threonine kinase domain whose enzymatic activity is regulated by blue light. The dark-adapted state crystal structures of the Arabidopsis thaliana phototropin 1 and phototropin 2 LOV1-domain constructs flanked by an N-terminal A'α helix and the structure of the phototropin 2 core LOV2 domain are known. Here, the crystal structure of the A. thaliana phototropin 1 LOV2 domain has been determined in its dark-adapted state. The core is flanked by an N-terminal A'α helix and a C-terminal Jα helix similar to those in the previously reported structure of Avena sativa phototropin 1 LOV2. In contrast to the monomeric A. sativa LOV2, A. thaliana LOV2 is a dimer in which two A'α helices adopt a scissor-like orientation at the dimer interface and form a short α-helical coiled coil. The Jα helix predominantly interacts with the β-sheet and plays a role in coiled-coil formation and dimerization.
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