ArticleScience advances2016
Structural photoactivation of a full-length bacterial phytochrome.
Article in Science advances, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 118 citations in OpenAlex.
- Deep learning for optoacoustic imaging of reversibly switchable proteins: training and performance testing using simulated multispectral optoacoustic tomography images.Journal of biomedical optics · 2026Article
- Assessing protein-specific radiation damage in time-resolved X-ray solution-scattering experiments at high-brilliance synchrotrons using fast detector readout.Acta crystallographica. Section D, Structural biology · 2026Article
- Time-resolved x-ray solution scattering from detergent solubilized visual rhodopsin.Biophysical journal · 2026Article
- Proton-Coupled Chromophore and Protein Structural Changes Control Phytochrome Activation.Biochemistry · 2026Article
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Chemical Mechanism of Allosteric and Asymmetric Dark Reversion in a Bacterial Phytochrome Uncovered by Cryo-EM.Journal of the American Chemical Society · 2025Article
- Deep-tissue high-sensitivity multimodal imaging and optogenetic manipulation enabled by biliverdin reductase knockout.Nature communications · 2025Article
- Observation of early events in the photoactivation of Myxobacterial phytochrome using time-resolved serial femtosecond crystallography.Communications chemistry · 2025Article
- Serial-femtosecond crystallography reveals how a phytochrome variant couples chromophore and protein structural changes.Science advances · 2025Article
- Engineered bacteria: Strategies and applications in cancer immunotherapy.Fundamental research · 2025Review
- Time-resolved X-ray solution scattering unveils the events leading to hemoglobin heme capture by staphylococcal IsdB.Nature communications · 2025Article
- Photoreception and signaling in bacterial phytochrome revealed by single-particle cryo-EM.Science advances · 2024Article
- Current Trends of Bacterial and Fungal Optoproteins for Novel Optical Applications.International journal of molecular sciences · 2023Review
- Osmolytes Modulate Photoactivation of Phytochrome: Probing Protein Hydration.Molecules (Basel, Switzerland) · 2023Article
- Erythroprotective Potential of Phycobiliproteins Extracted fromMetabolites · 2023Article
- Long-Distance Protonation-Conformation Coupling in Phytochrome Species.Molecules (Basel, Switzerland) · 2022Article
- Protein control of photochemistry and transient intermediates in phytochromes.Nature communications · 2022Article
- The structural effect between the output module and chromophore-binding domain is a two-way street via the hairpin extension.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
- Optogenetic Control of Bacterial Expression by Red Light.ACS synthetic biology · 2022Article
- Characterisation of sequence-structure-function space in sensor-effector integrators of phytochrome-regulated diguanylate cyclases.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2022Article
1 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
19 authors at 6 institutions in 5 countries.
Funding
Abstract
Phytochromes are light sensor proteins found in plants, bacteria, and fungi. They function by converting a photon absorption event into a conformational signal that propagates from the chromophore through the entire protein. However, the structure of the photoactivated state and the conformational changes that lead to it are not known. We report time-resolved x-ray scattering of the full-length phytochrome from Deinococcus radiodurans on micro- and millisecond time scales. We identify a twist of the histidine kinase output domains with respect to the chromophore-binding domains as the dominant change between the photoactivated and resting states. The time-resolved data further show that the structural changes up to the microsecond time scales are small and localized in the chromophore-binding domains. The global structural change occurs within a few milliseconds, coinciding with the formation of the spectroscopic meta-Rc state. Our findings establish key elements of the signaling mechanism of full-length bacterial phytochromes.
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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.