Structural insights into a secretory abundant heat‐soluble protein from an anhydrobiotic tardigrade, Ramazzottius varieornatus. Issue 16 (8th August 2017)

• Record Type: Journal Article
• Authors: Fukuda, Yohta; Miura, Yoshimasa; Mizohata, Eiichi; Inoue, Tsuyoshi
• Is Part Of: FEBS letters. Volume 591:Issue 16(2017)
• Page Start: 2458
• Page End: 2469
• Publication Date: 2017-08-08
• Subjects: crystal structure -- fatty acid‐binding protein -- secretory abundant heat‐soluble protein -- tardigrades; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1002/1873-3468.12752
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Upon 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 ( Rv SAHS1), which is one of the toughest tardigrades. Rv SAHS1 shows a β‐barrel structure similar to fatty acid‐binding proteins (FABPs), in which hydrophilic residues form peculiar hydrogen bond networks, which would provide Rv SAHS1 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. Abstract :