ArticleChemical science2021
The structural changes in the signaling mechanism of bacteriophytochromes in solution revealed by a multiscale computational investigation.
Article in Chemical science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Using Computational Techniques for the Characterization of Structural Changes During the Phytochrome Photocycle.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Analogies and Differences in the Photoactivation Mechanism of Bathy and Canonical Bacteriophytochromes Revealed by Multiscale Modeling.The journal of physical chemistry letters · 2024Article
- Long-Distance Protonation-Conformation Coupling in Phytochrome Species.Molecules (Basel, Switzerland) · 2022Article
- Protein control of photochemistry and transient intermediates in phytochromes.Nature communications · 2022Article
- Light-induced protein structural dynamics in bacteriophytochrome revealed by time-resolved x-ray solution scattering.Science advances · 2022Article
- Enhancing the Inhomogeneous Photodynamics of Canonical Bacteriophytochrome.The journal of physical chemistry. B · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phytochromes are red-light sensing proteins, with important light-regulatory roles in different organisms, which are capturing an increasing interest in bioimaging and optogenetics. Upon absorption of light by the embedded bilin chromophore, they undergo structural changes that extend from the chromophore to the protein and finally drive the biological function. Up to now, the underlying mechanism still has to be characterized fully. Here we investigate the Pfr activated form of a bacterial phytochrome, by combining extensive molecular dynamics simulations with a polarizable QM/MM description of the spectroscopic properties, revealing a large structure relaxation in solution, compared to the crystal structure, both in the chromophore-binding pocket and in the overall structure of the phytochrome. Our results indicate that the final opening of the dimeric structure is preceded by an important internal reorganization of the phytochrome specific (PHY) domain involving a bend of the helical spine connecting the PHY domain with the chromophore-binding domain, opening the way to a new understanding of the activation pathway.
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