ArticleScientific reports2019
X-ray Crystallographic Structure and Oligomerization of Gloeobacter Rhodopsin.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 69 citations in OpenAlex.
- Rhobot-Screen: an integrated robotic platform for functional screening of rhodopsin variants.BMC biology · 2026Article
- Article
- Opsins are Phospholipid Scramblases in All Domains of Life.bioRxiv : the preprint server for biology · 2025Article
- Significant Effects of Excitonic Coupling and Charge Transfer on the Circular Dichroism Spectrum of Photosynthetic Light-Harvesting I Complex.The journal of physical chemistry. B · 2025Article
- Proteorhodopsin insights into the molecular mechanism of vectorial proton transport.Science advances · 2025Article
- Structural insights into the mechanism and dynamics of proteorhodopsin biogenesis and retinal scavenging.Nature communications · 2024Article
- Molecular Mechanisms behind Circular Dichroism Spectral Variations between Channelrhodopsin and Heliorhodopsin Dimers.The journal of physical chemistry letters · 2024Article
- Impact of protein-chromophore interaction on the retinal excited state and photocycle ofChemical science · 2023Article
- Structures of channelrhodopsin paralogs in peptidiscs explain their contrasting KNature communications · 2023Article
- Retinal-Carotenoid Interactions in a Sodium-Ion-Pumping Rhodopsin: Implications on Oligomerization and Thermal Stability.The journal of physical chemistry. B · 2023Article
- Low pH structure of heliorhodopsin reveals chloride binding site and intramolecular signaling pathway.Scientific reports · 2022Article
- Genome Sequence and Characterization of a Xanthorhodopsin-Containing, Aerobic Anoxygenic PhototrophicMicroorganisms · 2022Article
- Rhodopsin-bestrophin fusion proteins from unicellular algae form gigantic pentameric ion channels.Nature structural & molecular biology · 2022Article
- Carotenoid binding in Gloeobacteria rhodopsin provides insights into divergent evolution of xanthorhodopsin types.Communications biology · 2022Article
- Coupling a Live Cell Directed Evolution Assay with Coevolutionary Landscapes to Engineer an Improved Fluorescent Rhodopsin Chloride Sensor.ACS synthetic biology · 2022Article
- Article
- Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Evaluation of protein descriptors in computer-aided rational protein engineering tasks and its application in property prediction in SARS-CoV-2 spike glycoprotein.Computational and structural biotechnology journal · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Crystallization of Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gloeobacter rhodopsin (GR) is a cyanobacterial proton pump which can be potentially applied to optogenetics. We solved the crystal structure of GR and found that it has overall similarity to the homologous proton pump from Salinibacter ruber, xanthorhodopsin (XR). We identified distinct structural characteristics of GR's hydrogen bonding network in the transmembrane domain as well as the displacement of extracellular sides of the transmembrane helices relative to those of XR. Employing Raman spectroscopy and flash-photolysis, we found that GR in the crystals exists in a state which displays retinal conformation and photochemical cycle similar to the functional form observed in lipids. Based on the crystal structure of GR, we selected a site for spin labeling to determine GR's oligomerization state using double electron-electron resonance (DEER) spectroscopy and demonstrated the pH-dependent pentamer formation of GR. Determination of the structure of GR as well as its pentamerizing propensity enabled us to reveal the role of structural motifs (extended helices, 3-omega motif and flipped B-C loop) commonly found among light-driven bacterial pumps in oligomer formation. Here we propose a new concept to classify these pumps based on the relationship between their oligomerization propensities and these structural determinants.
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