ArticleProceedings of the National Academy of Sciences of the United States of America2013
Crystal structure of the FRP and identification of the active site for modulation of OCP-mediated photoprotection in cyanobacteria.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 100 citations in OpenAlex.
- Molecular Mechanisms ofPlants (Basel, Switzerland) · 2025Review
- Light sensitive orange carotenoid proteins (OCPs) in cyanobacterial photoprotection: evolutionary insights, structural-functional dynamics and biotechnological prospects.Archives of microbiology · 2025Review
- Solution Structures of Two Different FRP-OCP Complexes as Revealed via SEC-SANS.International journal of molecular sciences · 2024Article
- Structure and function of the light-protective orange carotenoid protein families.Current research in structural biology · 2024Review
- Fortuitously compatible protein surfaces primed allosteric control in cyanobacterial photoprotection.Nature ecology & evolution · 2023Article
- Article
- Integrated Structural Studies for Elucidating Carotenoid-Protein Interactions.Advances in experimental medicine and biology · 2022Article
- Heterologous expression of cyanobacterial Orange Carotenoid Protein (OCP2) as a soluble carrier of ketocarotenoids inAlgal research · 2021Article
- The Role of Selected Wavelengths of Light in the Activity of Photosystem II inInternational journal of molecular sciences · 2021Article
- Molecular Mechanisms of Activation in the Orange Carotenoid Protein Revealed by Molecular Dynamics.Journal of the American Chemical Society · 2020Article
- Fluorescence recovery protein: a powerful yet underexplored regulator of photoprotection in cyanobacteria†.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2020Review
- Comparative ultrafast spectroscopy and structural analysis of OCP1 and OCP2 from Tolypothrix.Biochimica et biophysica acta. Bioenergetics · 2020Article
- An atypical short-chain dehydrogenase-reductase functions in the relaxation of photoprotective qH in Arabidopsis.Nature plants · 2020Article
- Interdomain interactions reveal the molecular evolution of the orange carotenoid protein.Nature plants · 2019Article
- X-ray radiolytic labeling reveals the molecular basis of orange carotenoid protein photoprotection and its interactions with fluorescence recovery protein.The Journal of biological chemistry · 2019Article
- Global Transcriptional Profiling of the CyanobacteriumFrontiers in microbiology · 2019Article
- OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria.Nature communications · 2018Article
- Site, trigger, quenching mechanism and recovery of non-photochemical quenching in cyanobacteria: recent updates.Photosynthesis research · 2018Review
- Photoprotective, excited-state quenching mechanisms in diverse photosynthetic organisms.The Journal of biological chemistry · 2018Review
- Interaction of the signaling state analog and the apoprotein form of the orange carotenoid protein with the fluorescence recovery protein.Photosynthesis research · 2018Article
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Photosynthetic reaction centers are sensitive to high light conditions, which can cause damage because of the formation of reactive oxygen species. To prevent high-light induced damage, cyanobacteria have developed photoprotective mechanisms. One involves a photoactive carotenoid protein that decreases the transfer of excess energy to the reaction centers. This protein, the orange carotenoid protein (OCP), is present in most cyanobacterial strains; it is activated by high light conditions and able to dissipate excess energy at the site of the light-harvesting antennae, the phycobilisomes. Restoration of normal antenna capacity involves the fluorescence recovery protein (FRP). The FRP acts to dissociate the OCP from the phycobilisomes by accelerating the conversion of the active red OCP to the inactive orange form. We have determined the 3D crystal structure of the FRP at 2.5 Å resolution. Remarkably, the FRP is found in two very different conformational and oligomeric states in the same crystal. Based on amino acid conservation analysis, activity assays of FRP mutants, FRP:OCP docking simulations, and coimmunoprecipitation experiments, we conclude that the dimer is the active form. The second form, a tetramer, may be an inactive form of FRP. In addition, we have identified a surface patch of highly conserved residues and shown that those residues are essential to FRP activity.
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