ArticleProtein science : a publication of the Protein Society2018
Crystal structure of secretory abundant heat soluble protein 4 from one of the toughest "water bears" micro-animals Ramazzottius Varieornatus.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed.
- Integrative bioinformatics analysis of potential convergent evolution in tardigrade stress-response proteins.Stress biology · 2026Article
- Tardigrades' cytoplasmic abundant heat soluble proteins serve as membrane protectors during dehydration.Research square · 2025Article
- Surviving desiccation: key factors underlying tolerance in prokaryotes and eukaryotes.Protoplasma · 2025Review
- Tardigrade secretory proteins protect biological structures from desiccation.Communications biology · 2024Article
- The major inducible small heat shock protein HSP20-3 in the tardigrade Ramazzottius varieornatus forms filament-like structures and is an active chaperone.Cell stress & chaperones · 2024Article
- Helicity of a tardigrade disordered protein contributes to its protective function during desiccation.Protein science : a publication of the Protein Society · 2024Article
- The Evolution of Temperature and Desiccation-Related Protein Families in Tardigrada Reveals a Complex Acquisition of Extremotolerance.Genome biology and evolution · 2024Article
- Structural insights into a C2 domain protein specifically found in tardigrades.Protein science : a publication of the Protein Society · 2021Article
- Architecture of Dispatched, a Transmembrane Protein Responsible for Hedgehog Release.Frontiers in molecular biosciences · 2021Article
- The biology of tardigrade disordered proteins in extreme stress tolerance.Cell communication and signaling : CCS · 2020Review
- Structure of cytochrome bProtein science : a publication of the Protein Society · 2020Article
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Abstract
Though anhydrobiotic tardigrades (micro-animals also known as water bears) possess many genes of secretory abundant heat soluble (SAHS) proteins unique to Tardigrada, their functions are unknown. A previous crystallographic study revealed that a SAHS protein (RvSAHS1) from one of the toughest tardigrades, Ramazzottius varieornatus, has a β-barrel architecture similar to fatty acid binding proteins (FABPs) and two putative ligand binding sites (LBS1 and LBS2) where fatty acids can bind. However, some SAHS proteins such as RvSAHS4 have different sets of amino acid residues at LBS1 and LBS2, implying that they prefer other ligands and have different functions. Here RvSAHS4 was crystallized and analyzed under a condition similar to that for RvSAHS1. There was no electron density corresponding to a fatty acid at LBS1 of RvSAHS4, where a putative fatty acid was observed in RvSAHS1. Instead, LBS2 of RvSAHS4, which was composed of uncharged residues, captured a putative polyethylene glycol molecule. These results suggest that RvSAHS4 mainly uses LBS2 for the binding of uncharged molecules.
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