ArticleProceedings of the National Academy of Sciences of the United States of America2001
X-ray structure of sensory rhodopsin II at 2.1-A resolution.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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Who cites it
79 citing papers in PubMed, 271 citations in OpenAlex.
- A quantum-mechanical framework for million-atom scale biological systems.Communications chemistry · 2026Article
- Surface Density-Dependent Interactions between Photoactivated Sensory Rhodopsin 2 and Its Transducer.ACS omega · 2026Article
- Bridging Quantum Mechanics and Biology at the Million-Atom Scale.Research square · 2025Article
- Rhodopsin charge diffusion computations disclose contrasting color-tuning mechanisms.Nature communications · 2025Article
- Structural basis for the prolonged photocycle of sensory rhodopsin II revealed by serial synchrotron crystallography.Nature communications · 2025Article
- Article
- Biophysical characterization of microbial rhodopsins with DSE motif.Biophysics and physicobiology · 2023Article
- 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
- Fake It 'Till You Make It-The Pursuit of Suitable Membrane Mimetics for Membrane Protein Biophysics.International journal of molecular sciences · 2020Review
- Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy.Angewandte Chemie (International ed. in English) · 2020Article
- Well-based crystallization of lipidic cubic phase microcrystals for serial X-ray crystallography experiments.Acta crystallographica. Section D, Structural biology · 2019Article
- Mimicking Microbial Rhodopsin Isomerization in a Single Crystal.Journal of the American Chemical Society · 2019Article
- Microbial Rhodopsins: Diversity, Mechanisms, and Optogenetic Applications.Annual review of biochemistry · 2017Review
- New Insights on Signal Propagation by Sensory Rhodopsin II/Transducer Complex.Scientific reports · 2017Article
- Article
- Structure of an Inward Proton-Transporting Anabaena Sensory Rhodopsin Mutant: Mechanistic Insights.Biophysical journal · 2016Article
- Lipidic cubic phase injector is a viable crystal delivery system for time-resolved serial crystallography.Nature communications · 2016Article
- Atomistic design of microbial opsin-based blue-shifted optogenetics tools.Nature communications · 2015Article
- In situ structural studies of Anabaena sensory rhodopsin in the E. coli membrane.Biophysical journal · 2015Article
19 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sensory rhodopsins (SRs) belong to a subfamily of heptahelical transmembrane proteins containing a retinal chromophore. These photoreceptors mediate the cascade of vision in animal eyes and phototaxis in archaebacteria and unicellular flagellated algae. Signal transduction by these photoreceptors occurs by means of transducer proteins. The two archaebacterial sensory rhodopsins SRI and SRII are coupled to the membrane-bound HtrI and HtrII transducer proteins. Activation of these proteins initiates phosphorylation cascades that modulate the flagellar motors, resulting in either attractant (SRI) or repellent (SRII) phototaxis. In addition, transducer-free SRI and SRII were shown to operate as proton pumps, analogous to bacteriorhodopsin. Here, we present the x-ray structure of SRII from Natronobacterium pharaonis (pSRII) at 2.1-A resolution, revealing a unique molecular architecture of the retinal-binding pocket. In particular, the structure of pSRII exhibits a largely unbent conformation of the retinal (as compared with bacteriorhodopsin and halorhodopsin), a hydroxyl group of Thr-204 in the vicinity of the Schiff base, and an outward orientation of the guanidinium group of Arg-72. Furthermore, the structure reveals a putative chloride ion that is coupled to the Schiff base by means of a hydrogen-bond network and a unique, positively charged surface patch for a probable interaction with HtrII. The high-resolution structure of pSRII provides a structural basis to elucidate the mechanisms of phototransduction and color tuning.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.