ArticleNature2010
Structural basis for the photoconversion of a phytochrome to the activated Pfr form.
Article in Nature, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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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.
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Who cites it
47 citing papers in PubMed, 138 citations in OpenAlex.
- Role of Nuclear Motion in the Ultrafast Relaxation Dynamics of Inner-Shell Vacancies in Hydrated Pyrrole.The journal of physical chemistry. A · 2026Article
- A PIF-regulated switch in cell axis growth drives cotyledon expansion through tissue-specific cell expansion and division.The Plant journal : for cell and molecular biology · 2025Article
- Crystal structure of the photosensory module from a PAS-less cyanobacterial phytochrome as Pr shows a mix of dark-adapted and photoactivated features.The Journal of biological chemistry · 2024Article
- Light signaling in plants-a selective history.Plant physiology · 2024Review
- Modulation of biliverdin dynamics and spectral properties by Sandercyanin.RSC advances · 2022Article
- Optophysiology: Illuminating cell physiology with optogenetics.Physiological reviews · 2022Review
- Light- and pH-dependent structural changes in cyanobacteriochrome AnPixJg2.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Amino Acid Signaling for TOR in Eukaryotes: Sensors, Transducers, and a Sustainable Agricultural fuTORe.Biomolecules · 2022Review
- The Red Edge: Bilin-Binding Photoreceptors as Optogenetic Tools and Fluorescence Reporters.Chemical reviews · 2021Review
- Far-red light acclimation in diverse oxygenic photosynthetic organisms.Photosynthesis research · 2019Review
- Light-induced complex formation of bacteriophytochrome RpBphP1 and gene repressor RpPpsR2 probed by SAXS.The FEBS journal · 2019Article
- Plant Phytochromes and their Phosphorylation.International journal of molecular sciences · 2019Review
- Influence of the N-terminal segment and the PHY-tongue element on light-regulation in bacteriophytochromes.The Journal of biological chemistry · 2019Article
- 3D Structures of Plant Phytochrome A as Pr and Pfr From Solid-State NMR: Implications for Molecular Function.Frontiers in plant science · 2018Article
- Mapping light-driven conformational changes within the photosensory module of plant phytochrome B.Scientific reports · 2016Article
- Perception of the plant hormone ethylene: known-knowns and known-unknowns.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
- Arabidopsis atypical kinase ABC1K1 is involved in red light-mediated development.Plant cell reports · 2016Article
- Identification of a new electron-transfer relaxation pathway in photoexcited pyrrole dimers.Nature communications · 2016Article
- X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. radiodurans phytochrome.Journal of the American Chemical Society · 2015Article
- Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1).The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Phytochromes are a collection of bilin-containing photoreceptors that regulate numerous photoresponses in plants and microorganisms through their ability to photointerconvert between a red-light-absorbing, ground state (Pr) and a far-red-light-absorbing, photoactivated state (Pfr). Although the structures of several phytochromes as Pr have been determined, little is known about the structure of Pfr and how it initiates signalling. Here we describe the three-dimensional solution structure of the bilin-binding domain as Pfr, using the cyanobacterial phytochrome from Synechococcus OSB'. Contrary to predictions, light-induced rotation of the A pyrrole ring but not the D ring is the primary motion of the chromophore during photoconversion. Subsequent rearrangements within the protein then affect intradomain and interdomain contact sites within the phytochrome dimer. On the basis of our models, we propose that phytochromes act by propagating reversible light-driven conformational changes in the bilin to altered contacts between the adjacent output domains, which in most phytochromes direct differential phosphotransfer.
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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.