5xn9
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Crystal structure of a secretary abundant heat soluble (SAHS) protein from Ramazzottius varieornatus (from monomer sample)== | |
+ | <StructureSection load='5xn9' size='340' side='right' caption='[[5xn9]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5xn9]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XN9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XN9 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xn9 OCA], [http://pdbe.org/5xn9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xn9 RCSB], [http://www.ebi.ac.uk/pdbsum/5xn9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xn9 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/SAHS1_RAMVA 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]<ref>PMID:22937162</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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 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<ref>PMID:28703282</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 5xn9" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Fukuda, Y]] | [[Category: Fukuda, Y]] | ||
+ | [[Category: Inoue, T]] | ||
[[Category: Miura, Y]] | [[Category: Miura, Y]] | ||
+ | [[Category: Mizohata, E]] | ||
+ | [[Category: Fatty acid binding protein]] | ||
+ | [[Category: Lipid transport]] | ||
+ | [[Category: Ramazzottius varieornatus]] | ||
+ | [[Category: Secretary abundant heat soluble protein]] |
Revision as of 03:44, 6 September 2017
Crystal structure of a secretary abundant heat soluble (SAHS) protein from Ramazzottius varieornatus (from monomer sample)
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