13kw: Difference between revisions
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==Human Single-ring Hsp10== | |||
<StructureSection load='13kw' size='340' side='right'caption='[[13kw]], [[Resolution|resolution]] 4.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[13kw]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=13KW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=13KW FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</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=13kw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=13kw OCA], [https://pdbe.org/13kw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=13kw RCSB], [https://www.ebi.ac.uk/pdbsum/13kw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=13kw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CH10_HUMAN CH10_HUMAN] Eukaryotic CPN10 homolog which is essential for mitochondrial protein biogenesis, together with CPN60. Binds to CPN60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The human chaperone complex Hsp60/Hsp10 is essential for maintaining cellular proteostasis by preventing protein misfolding and aggregation. Disruption of these processes contributes to neurodegenerative diseases, while overexpression of Hsp60 and Hsp10 is associated with various cancers. Understanding their molecular mechanisms is therefore of fundamental importance. Unlike its bacterial homolog GroEL, human Hsp60 adopts multiple oligomeric states, with both heptameric and tetradecameric forms binding Hsp10 to form a folding cavity for substrate refolding. Here, we determine the cryo-EM structure of apo Hsp10 and find that, in addition to its single-ring form, it also assembles into a compact double-ring state. This reveals that Hsp10, like Hsp60, exhibits structural behavior that differs markedly from its bacterial counterpart. Traditionally viewed as a passive cofactor assisting Hsp60, we show that Hsp10 alone possesses intrinsic chaperone activity: it supports folding of natural substrates such as malate dehydrogenase 1 and manganese superoxide dismutase. NMR analysis further shows that substrate binding occurs primarily at the core of Hsp10 rather than at the loops. Our findings suggest that Hsp10 exists in equilibrium between single- and double-ring complexes in the unbound state, and upon binding as a single-ring complex, it actively guides substrates into the folding chamber. | |||
Hsp10: From Single to Double Rings-Structural Basis of Protein Homeostasis.,Page A, Hendricks W, Dunckley A, Walti MA bioRxiv [Preprint]. 2026 May 14:2026.05.12.724654. doi: , 10.64898/2026.05.12.724654. PMID:42182213<ref>PMID:42182213</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 13kw" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Page AA]] | |||
[[Category: Walti MA]] | |||
