ArticleScience advances2024
Molecular mechanisms and evolutionary robustness of a color switch in proteorhodopsins.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Characterization of Full-Length Antibody Complexes Through HDX-Mass Spectrometry Coupled With NMR Spectroscopy: New Insight Into Avelumab/PD-L1 Interaction.Angewandte Chemie (International ed. in English) · 2026Article
- Atomic structure and dynamics of the mechanosensitive channel MscL fromScience advances · 2026Article
- Article
- Opsins are Phospholipid Scramblases in All Domains of Life.bioRxiv : the preprint server for biology · 2025Article
- Structural Transition from Closed to Open for the Influenza A M2 Proton Channel as Observed by Proton-Detected Solid-State NMR.Journal of the American Chemical Society · 2025Article
- Dynamic nuclear polarization and chemically induced hyperpolarization: Progress, mechanisms, and opportunities.Magnetic resonance letters · 2025Review
- Rhodopsin charge diffusion computations disclose contrasting color-tuning mechanisms.Nature communications · 2025Article
- Structural insights into the mechanism and dynamics of proteorhodopsin biogenesis and retinal scavenging.Nature communications · 2024Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteorhodopsins are widely distributed photoreceptors from marine bacteria. Their discovery revealed a high degree of evolutionary adaptation to ambient light, resulting in blue- and green-absorbing variants that correlate with a conserved glutamine/leucine at position 105. On the basis of an integrated approach combining sensitivity-enhanced solid-state nuclear magnetic resonance (ssNMR) spectroscopy and linear-scaling quantum mechanics/molecular mechanics (QM/MM) methods, this single residue is shown to be responsible for a variety of synergistically coupled structural and electrostatic changes along the retinal polyene chain, ionone ring, and within the binding pocket. They collectively explain the observed color shift. Furthermore, analysis of the differences in chemical shift between nuclei within the same residues in green and blue proteorhodopsins also reveals a correlation with the respective degree of conservation. Our data show that the highly conserved color change mainly affects other highly conserved residues, illustrating a high degree of robustness of the color phenotype to sequence variation.
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