ArticleNature communications2020
Structural insights into the mechanism of rhodopsin phosphodiesterase.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
- CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments.Science advances · 2025Article
- Retinal to Retinal Energy Transfer in a Bistable Microbial Rhodopsin Dimer.Journal of the American Chemical Society · 2025Article
- Multicellularity and Electrical Forces.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025Review
- Plastid-localized xanthorhodopsin increases diatom biomass and ecosystem productivity in iron-limited surface oceans.Nature microbiology · 2023Article
- NaMolecules (Basel, Switzerland) · 2023Review
- Rhodopsin-bestrophin fusion proteins from unicellular algae form gigantic pentameric ion channels.Nature structural & molecular biology · 2022Article
- Characterization and Modification of Light-Sensitive Phosphodiesterases from Choanoflagellates.Biomolecules · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Crystallization of Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021Review
- Bioluminescence and Photoreception in Unicellular Organisms: Light-Signalling in a Bio-Communication Perspective.International journal of molecular sciences · 2021Review
- Article
- Guidelines for de novo phasing using multiple small-wedge data collection.Journal of synchrotron radiation · 2021Article
- Accurate Prediction of Absorption Spectral Shifts of Proteorhodopsin Using a Fragment-Based Quantum Mechanical Method.Molecules (Basel, Switzerland) · 2021Article
- Crystal structure of schizorhodopsin reveals mechanism of inward proton pumping.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Far-Red Absorbing Rhodopsins, Insights From Heterodimeric Rhodopsin-Cyclases.Frontiers in molecular biosciences · 2021Review
- Advances, Perspectives and Potential Engineering Strategies of Light-Gated Phosphodiesterases for Optogenetic Applications.International journal of molecular sciences · 2020Review
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rhodopsin phosphodiesterase (Rh-PDE) is an enzyme rhodopsin belonging to a recently discovered class of microbial rhodopsins with light-dependent enzymatic activity. Rh-PDE consists of the N-terminal rhodopsin domain and C-terminal phosphodiesterase (PDE) domain, connected by 76-residue linker, and hydrolyzes both cAMP and cGMP in a light-dependent manner. Thus, Rh-PDE has potential for the optogenetic manipulation of cyclic nucleotide concentrations, as a complementary tool to rhodopsin guanylyl cyclase and photosensitive adenylyl cyclase. Here we present structural and functional analyses of the Rh-PDE derived from Salpingoeca rosetta. The crystal structure of the rhodopsin domain at 2.6 Å resolution revealed a new topology of rhodopsins, with 8 TMs including the N-terminal extra TM, TM0. Mutational analyses demonstrated that TM0 plays a crucial role in the enzymatic photoactivity. We further solved the crystal structures of the rhodopsin domain (3.5 Å) and PDE domain (2.1 Å) with their connecting linkers, which showed a rough sketch of the full-length Rh-PDE. Integrating these structures, we proposed a model of full-length Rh-PDE, based on the HS-AFM observations and computational modeling of the linker region. These findings provide insight into the photoactivation mechanisms of other 8-TM enzyme rhodopsins and expand the definition of rhodopsins.
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