Structural highlights
Function[SAHS1_RAMVA] Secreted heat soluble protein acting as a molecular shield in water-deficient condition (PubMed:22937162). Tardigrade-specific intrinsically disordered proteins (TDPs) are essential for desiccation tolerance by forming non-crystalline amorphous solids upon desiccation, and this vitrified state mirrors their protective capabilities (By similarity).[UniProtKB:P0CU39][1] Publication Abstract from PubMedUpon stopping metabolic processes, some tardigrades can undergo anhydrobiosis. Secretory abundant heat-soluble (SAHS) proteins have been reported as candidates for anhydrobiosis-related proteins in tardigrades, which seem to protect extracellular components and/or secretory organelles. We determined structures of a SAHS protein from Ramazzottius varieornatus (RvSAHS1), which is one of the toughest tardigrades. RvSAHS1 shows a beta-barrel structure similar to fatty acid-binding proteins (FABPs), in which hydrophilic residues form peculiar hydrogen bond networks, which would provide RvSAHS1 with better tolerance against dehydration. We identified two putative ligand-binding sites: one that superimposes on those of some FABPs and the other, unique to and conserved in SAHS proteins. These results indicate that SAHS proteins constitute a new FABP family. Structural insights into a secretory abundant heat-soluble protein from an anhydrobiotic tardigrade, Ramazzottius varieornatus.,Fukuda Y, Miura Y, Mizohata E, Inoue T FEBS Lett. 2017 Aug;591(16):2458-2469. doi: 10.1002/1873-3468.12752. Epub 2017, Aug 8. PMID:28703282[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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