ArticleNature communications2021
Structures of the archaerhodopsin-3 transporter reveal that disordering of internal water networks underpins receptor sensitization.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Expanding the Reach of Membrane Protein-Ligand Interaction Studies Through the Integration of Mass Spectrometry and Membrane Mimetics.Proteomics · 2025Review
- Rhodopsin charge diffusion computations disclose contrasting color-tuning mechanisms.Nature communications · 2025Article
- Proteorhodopsin insights into the molecular mechanism of vectorial proton transport.Science advances · 2025Article
- Article
- Elucidation of Expression Patterns and Functional Properties of Archaerhodopsin Derived fromBiology · 2025Article
- Rational Design of Far-Red Archaerhodopsin-3-Based Fluorescent Genetically Encoded Voltage Indicators: from Elucidation of the Fluorescence Mechanism in Archers to Novel Red-Shifted Variants.ACS physical chemistry Au · 2024Article
- Crystallographic insights into lipid-membrane protein interactions in microbial rhodopsins.Frontiers in molecular biosciences · 2024Article
- A versatile approach to high-density microcrystals in lipidic cubic phase for room-temperature serial crystallography.Journal of applied crystallography · 2023Article
- A comparative characterisation of commercially available lipid-polymer nanoparticles formed from model membranes.European biophysics journal : EBJ · 2023Article
- QuasAr Odyssey: the origin of fluorescence and its voltage sensitivity in microbial rhodopsins.Nature communications · 2022Article
- Parallel transmission in a synthetic nerve.Nature chemistry · 2022Article
- True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins.Nature structural & molecular biology · 2022Article
- Graphs of protein-water hydrogen bond networks to dissect structural movies of ion-transfer microbial rhodopsins.Frontiers in chemistry · 2022Article
- Rhodopsins: An Excitingly Versatile Protein Species for Research, Development and Creative Engineering.Frontiers in chemistry · 2022Review
- Hypersaline environments as natural sources of microbes with potential applications in biotechnology: The case of solar evaporation systems to produce salt in Alicante County (Spain).Current research in microbial sciences · 2022Review
- Crystallization of Microbial Rhodopsins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Two states of a light-sensitive membrane protein captured at room temperature using thin-film sample mounts.Acta crystallographica. Section D, Structural biology · 2022Article
- Photoactivation of Cell-Free Expressed Archaerhodopsin-3 in a Model Cell Membrane.International journal of molecular sciences · 2021Article
- Optical Switching Between Long-lived States of Opsin Transmembrane Voltage Sensors.Photochemistry and photobiology · 2021Article
- Finding the Spark.Bioelectricity · 2021Article
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15 authors.
Funding
Abstract
Many transmembrane receptors have a desensitized state, in which they are unable to respond to external stimuli. The family of microbial rhodopsin proteins includes one such group of receptors, whose inactive or dark-adapted (DA) state is established in the prolonged absence of light. Here, we present high-resolution crystal structures of the ground (light-adapted) and DA states of Archaerhodopsin-3 (AR3), solved to 1.1 Å and 1.3 Å resolution respectively. We observe significant differences between the two states in the dynamics of water molecules that are coupled via H-bonds to the retinal Schiff Base. Supporting QM/MM calculations reveal how the DA state permits a thermodynamic equilibrium between retinal isomers to be established, and how this same change is prevented in the ground state in the absence of light. We suggest that the different arrangement of internal water networks in AR3 is responsible for the faster photocycle kinetics compared to homologs.
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