5XNA
Crystal structure of a secretary abundant heat soluble (SAHS) protein from Ramazzottius varieornatus (from dimer sample)
Summary for 5XNA
| Entry DOI | 10.2210/pdb5xna/pdb |
| Descriptor | SAHS1, ZINC ION, MAGNESIUM ION, ... (8 entities in total) |
| Functional Keywords | secretary abundant heat soluble protein, ramazzottius varieornatus, fatty acid binding protein, lipid transport |
| Biological source | Ramazzottius varieornatus (Water bear) |
| Total number of polymer chains | 2 |
| Total formula weight | 33952.87 |
| Authors | Fukuda, Y.,Miura, Y.,Mizohata, E.,Inoue, T. (deposition date: 2017-05-19, release date: 2017-07-26, Last modification date: 2024-03-27) |
| Primary citation | Fukuda, Y.,Miura, Y.,Mizohata, E.,Inoue, T. Structural insights into a secretory abundant heat-soluble protein from an anhydrobiotic tardigrade, Ramazzottius varieornatus FEBS Lett., 591:2458-2469, 2017 Cited by PubMed 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 (RvSAHS1), which is one of the toughest tardigrades. RvSAHS1 shows a β-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. PubMed: 28703282DOI: 10.1002/1873-3468.12752 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.802 Å) |
Structure validation
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