ArticleeLife2020
The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser.
Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 119 citations in OpenAlex.
- Refinement of amino-acid conformation vs. difference density maps in time-resolved serial femtosecond crystallography data analysis.FEBS open bio · 2026Article
- Proton-Coupled Chromophore and Protein Structural Changes Control Phytochrome Activation.Biochemistry · 2026Article
- Plant structural biology: Emerging technologies and future biological insights.The Plant journal : for cell and molecular biology · 2026Review
- Advances in Crystallography and Cryo-Electron Microscopy for the Study of Membrane Proteins.Advances in experimental medicine and biology · 2026Review
- Photoisomerization of phytochrome's chromophore: a vibrational spectroscopic view on the primary ground state processes.RSC advances · 2025Article
- Ultrafast, remote-controlled protonation reaction enables structural changes in a phytochrome.Science advances · 2025Article
- Semi-automated modeling of reaction states in time-resolved serial femtosecond crystallography using molecular dynamics sampled conformations.Structural dynamics (Melville, N.Y.) · 2025Article
- Distinct Protochromic Mechanisms Driving Green/Red Absorption in Phycocyanobilin-Binding Proteins.Biochemistry · 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
- Article
- Structural effects of high laser power densities on an early bacteriorhodopsin photocycle intermediate.Nature communications · 2024Article
- ResiDEM: Analytical Tool for Isomorphous Difference Electron Density Maps Utilizing Dynamic Residue Identification via Density Clustering.Journal of chemical information and modeling · 2024Article
- Molecular origins of absorption wavelength variation among phycocyanobilin-binding proteins.Biophysical journal · 2024Article
- Analogies and Differences in the Photoactivation Mechanism of Bathy and Canonical Bacteriophytochromes Revealed by Multiscale Modeling.The journal of physical chemistry letters · 2024Article
- Appraising protein conformational changes by resampling time-resolved serial x-ray crystallography data.Structural dynamics (Melville, N.Y.) · 2024Article
- Directed ultrafast conformational changes accompany electron transfer in a photolyase as resolved by serial crystallography.Nature chemistry · 2024Article
- The time revolution in macromolecular crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
- Article
- Blue and red in the protein world: Photoactive yellow protein and phytochromes as revealed by time-resolved crystallography.Structural dynamics (Melville, N.Y.) · 2024Article
Corrections and comments
- Commented on byRapid response.2020
Authors and funding
30 authors at 8 institutions in 4 countries.
Funding
Abstract
Phytochrome proteins control the growth, reproduction, and photosynthesis of plants, fungi, and bacteria. Light is detected by a bilin cofactor, but it remains elusive how this leads to activation of the protein through structural changes. We present serial femtosecond X-ray crystallographic data of the chromophore-binding domains of a bacterial phytochrome at delay times of 1 ps and 10 ps after photoexcitation. The data reveal a twist of the D-ring, which leads to partial detachment of the chromophore from the protein. Unexpectedly, the conserved so-called pyrrole water is photodissociated from the chromophore, concomitant with movement of the A-ring and a key signaling aspartate. The changes are wired together by ultrafast backbone and water movements around the chromophore, channeling them into signal transduction towards the output domains. We suggest that the observed collective changes are important for the phytochrome photoresponse, explaining the earliest steps of how plants, fungi and bacteria sense red light.
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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.