ArticleScientific reports2016
Structure of a Highly Active Cephalopod S-crystallin Mutant: New Molecular Evidence for Evolution from an Active Enzyme into Lens-Refractive Protein.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 16 citations in OpenAlex.
- Article
- A single-cell atlas of the bobtail squid visual and nervous system highlights molecular principles of convergent evolution.Nature ecology & evolution · 2025Article
- Structural insights into sigma class glutathione transferase from Taenia solium: Analysis and functional implications.PLoS neglected tropical diseases · 2025Article
- Genomes of Two Flying Squid Species Provide Novel Insights into Adaptations of Cephalopods to Pelagic Life.Genomics, proteomics & bioinformatics · 2022Article
- Manipulating polydispersity of lens β-crystallins using divalent cations demonstrates evidence of calcium regulation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Dynamic pigmentary and structural coloration within cephalopod chromatophore organs.Nature communications · 2019Article
- Protein refractive index increment is determined by conformation as well as composition.Journal of physics. Condensed matter : an Institute of Physics journal · 2018Article
- Structure of HIV TAR in complex with a Lab-Evolved RRM provides insight into duplex RNA recognition and synthesis of a constrained peptide that impairs transcription.Nucleic acids research · 2018Article
- Dietary Effect on the Proteome of the Common Octopus (Frontiers in physiology · 2017Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Crystallins are found widely in animal lenses and have important functions due to their refractive properties. In the coleoid cephalopods, a lens with a graded refractive index provides good vision and is required for survival. Cephalopod S-crystallin is thought to have evolved from glutathione S-transferase (GST) with various homologs differentially expressed in the lens. However, there is no direct structural information that helps to delineate the mechanisms by which S-crystallin could have evolved. Here we report the structural and biochemical characterization of novel S-crystallin-glutathione complex. The 2.35-Å crystal structure of a S-crystallin mutant from Octopus vulgaris reveals an active-site architecture that is different from that of GST. S-crystallin has a preference for glutathione binding, although almost lost its GST enzymatic activity. We've also identified four historical mutations that are able to produce a "GST-like" S-crystallin that has regained activity. This protein recapitulates the evolution of S-crystallin from GST. Protein stability studies suggest that S-crystallin is stabilized by glutathione binding to prevent its aggregation; this contrasts with GST-σ, which do not possess this protection. We suggest that a tradeoff between enzyme activity and the stability of the lens protein might have been one of the major driving force behind lens evolution.
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