5xna: Difference between revisions
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==Crystal structure of a secretary abundant heat soluble (SAHS) protein from Ramazzottius varieornatus (from dimer sample)== | |||
<StructureSection load='5xna' size='340' side='right' caption='[[5xna]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5xna]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XNA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XNA 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=SHV:HEPTANOIC+ACID'>SHV</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=5xna FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xna OCA], [http://pdbe.org/5xna PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xna RCSB], [http://www.ebi.ac.uk/pdbsum/5xna PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xna 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> | |||
[[Category: | <div class="pdbe-citations 5xna" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Fukuda, Y]] | |||
[[Category: Inoue, T]] | [[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]] | |||
