3aab: Difference between revisions

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<StructureSection load='3aab' size='340' side='right'caption='[[3aab]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='3aab' size='340' side='right'caption='[[3aab]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3aab]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulto Sulto]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AAB FirstGlance]. <br>
<table><tr><td colspan='2'>[[3aab]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfurisphaera_tokodaii_str._7 Sulfurisphaera tokodaii str. 7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AAB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.851&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3aac|3aac]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ST1653 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=273063 SULTO])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3aab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aab OCA], [https://pdbe.org/3aab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aab RCSB], [https://www.ebi.ac.uk/pdbsum/3aab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aab ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3aab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aab OCA], [https://pdbe.org/3aab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aab RCSB], [https://www.ebi.ac.uk/pdbsum/3aab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aab ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q970D9_SULTO Q970D9_SULTO]
Small heat shock proteins (sHsps), which are categorized into a class of molecular chaperones, bind and stabilize denatured proteins to prevent aggregation. The sHsps undergo transition between different oligomeric states to control their hydrophobicity. So far, only the structures of sHsps in large oligomeric states have been reported. Here we report the structure of StHsp14.0 from Sulfolobus tokodaii in the dimeric state, which is formed by means of a mutation at the C-terminal IXI/V motif. The dimer is the sole building block in two crystal forms, and the dimeric mode is the same as that in the large oligomers. The N-terminal helix has variety in its conformation. Furthermore, spectroscopic and biochemical experiments were performed to investigate the conformational variability at the N-terminus. The structural, dynamical and oligomeric properties suggest that chaperone activity of StHsp14.0 is mediated by partially dissolved oligomers.


Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein, StHsp14.0.,Takeda K, Hayashi T, Abe T, Hirano Y, Hanazono Y, Yohda M, Miki K J Struct Biol. 2010 Dec 30. PMID:21195185<ref>PMID:21195185</ref>
==See Also==
 
*[[Heat Shock Protein structures|Heat Shock Protein structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3aab" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Sulto]]
[[Category: Sulfurisphaera tokodaii str. 7]]
[[Category: Abe, T]]
[[Category: Abe T]]
[[Category: Hanazono, Y]]
[[Category: Hanazono Y]]
[[Category: Hayashi, T]]
[[Category: Hayashi T]]
[[Category: Hirano, Y]]
[[Category: Hirano Y]]
[[Category: Miki, K]]
[[Category: Miki K]]
[[Category: Takeda, K]]
[[Category: Takeda K]]
[[Category: Yohda, M]]
[[Category: Yohda M]]
[[Category: Alpha-crystallin domain]]
[[Category: Chaperone]]
Retrieved from "https://proteopedia.org/3aab"