3vqk: Difference between revisions
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== | ==Small heat shock protein hsp14.0 of wild type== | ||
[[3vqk]] is a 6 chain structure with sequence from [ | <StructureSection load='3vqk' size='340' side='right'caption='[[3vqk]], [[Resolution|resolution]] 4.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vqk]] is a 6 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=3VQK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VQK FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.5Å</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=3vqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vqk OCA], [https://pdbe.org/3vqk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vqk RCSB], [https://www.ebi.ac.uk/pdbsum/3vqk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vqk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q970D9_SULTO Q970D9_SULTO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The small heat shock proteins (sHsps), which are widely found in all domains of life, bind and stabilize denatured proteins to prevent aggregation. The sHsps exist as large oligomers that are composed of 9-40 subunits and control their chaperone activity by the transition of the oligomeric state. Though the oligomeric transition is important for the biological function of most sHsps, atomic details have not been elucidated. Here, we report crystal structures in both the 24-meric and dimeric states for an sHsp, StHsp14.0 from Sulfolobus tokodaii, in order to reveal changes upon the oligomeric transition. The results indicate that StHsp14.0 forms a spherical 24-mer with a diameter of 115 A. The diameter is defined by the inter-monomer angle in the dimer. The dimer structure in the dimeric state shows only small differences from that in the 24-meric state. Some significant differences are exclusively observed at the binding site for the C-terminus. Although a dimer has four interactive sites with neighboring dimers, the weakness of the respective interactions is indicated from the size-exclusion chromatography. The small structural changes imply an activation mechanism mediated by multiple weak interactions. | |||
Structural Studies on the Oligomeric Transition of a Small Heat Shock Protein, StHsp14.0.,Hanazono Y, Takeda K, Yohda M, Miki K J Mol Biol. 2012 May 18. PMID:22613762<ref>PMID:22613762</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
[[Category: | <div class="pdbe-citations 3vqk" style="background-color:#fffaf0;"></div> | ||
[[Category: Hanazono | == References == | ||
[[Category: Miki | <references/> | ||
[[Category: Takeda | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sulfurisphaera tokodaii str. 7]] | |||
[[Category: Hanazono Y]] | |||
[[Category: Miki K]] | |||
[[Category: Takeda K]] | |||
Latest revision as of 15:33, 8 November 2023
Small heat shock protein hsp14.0 of wild typeSmall heat shock protein hsp14.0 of wild type
Structural highlights
FunctionPublication Abstract from PubMedThe small heat shock proteins (sHsps), which are widely found in all domains of life, bind and stabilize denatured proteins to prevent aggregation. The sHsps exist as large oligomers that are composed of 9-40 subunits and control their chaperone activity by the transition of the oligomeric state. Though the oligomeric transition is important for the biological function of most sHsps, atomic details have not been elucidated. Here, we report crystal structures in both the 24-meric and dimeric states for an sHsp, StHsp14.0 from Sulfolobus tokodaii, in order to reveal changes upon the oligomeric transition. The results indicate that StHsp14.0 forms a spherical 24-mer with a diameter of 115 A. The diameter is defined by the inter-monomer angle in the dimer. The dimer structure in the dimeric state shows only small differences from that in the 24-meric state. Some significant differences are exclusively observed at the binding site for the C-terminus. Although a dimer has four interactive sites with neighboring dimers, the weakness of the respective interactions is indicated from the size-exclusion chromatography. The small structural changes imply an activation mechanism mediated by multiple weak interactions. Structural Studies on the Oligomeric Transition of a Small Heat Shock Protein, StHsp14.0.,Hanazono Y, Takeda K, Yohda M, Miki K J Mol Biol. 2012 May 18. PMID:22613762[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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