7cg3: Difference between revisions
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<StructureSection load='7cg3' size='340' side='right'caption='[[7cg3]], [[Resolution|resolution]] 5.10Å' scene=''> | <StructureSection load='7cg3' size='340' side='right'caption='[[7cg3]], [[Resolution|resolution]] 5.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CG3 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.1Å</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=7cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cg3 OCA], [https://pdbe.org/7cg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cg3 RCSB], [https://www.ebi.ac.uk/pdbsum/7cg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cg3 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=7cg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cg3 OCA], [https://pdbe.org/7cg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cg3 RCSB], [https://www.ebi.ac.uk/pdbsum/7cg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cg3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 7cg3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7cg3" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Heat Shock Protein structures|Heat Shock Protein structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hanazono | [[Category: Hanazono Y]] | ||
[[Category: Harada | [[Category: Harada R]] | ||
[[Category: Inoue | [[Category: Inoue Y]] | ||
[[Category: Iwamasa | [[Category: Iwamasa N]] | ||
[[Category: Kawamoto | [[Category: Kawamoto A]] | ||
[[Category: Kimatsuka | [[Category: Kimatsuka M]] | ||
[[Category: Miki | [[Category: Miki K]] | ||
[[Category: Namba | [[Category: Namba K]] | ||
[[Category: Noguchi | [[Category: Noguchi K]] | ||
[[Category: Noi | [[Category: Noi K]] | ||
[[Category: Ogura | [[Category: Ogura T]] | ||
[[Category: Shibata | [[Category: Shibata K]] | ||
[[Category: Shigeta | [[Category: Shigeta Y]] | ||
[[Category: Shinohara | [[Category: Shinohara K]] | ||
[[Category: Takeda | [[Category: Takeda K]] | ||
[[Category: Yohda | [[Category: Yohda M]] | ||
Latest revision as of 22:30, 29 May 2024
Staggered ring conformation of CtHsp104 (Hsp104 from Chaetomium Thermophilum)Staggered ring conformation of CtHsp104 (Hsp104 from Chaetomium Thermophilum)
Structural highlights
Publication Abstract from PubMedHsp104 and its bacterial homolog ClpB form hexameric ring structures and mediate protein disaggregation. The disaggregated polypeptide is thought to thread through the central channel of the ring. However, the dynamic behavior of Hsp104 during disaggregation remains unclear. Here, we reported the stochastic conformational dynamics and a split conformation of Hsp104 disaggregase from Chaetomium thermophilum (CtHsp104) in the presence of ADP by X-ray crystallography, cryo-electron microscopy (EM), and high-speed atomic force microscopy (AFM). ADP-bound CtHsp104 assembles into a 65 left-handed spiral filament in the crystal structure at a resolution of 2.7 A. The unit of the filament is a hexamer of the split spiral structure. In the cryo-EM images, staggered and split hexameric rings were observed. Further, high-speed AFM observations showed that a substrate addition enhanced the conformational change and increased the split structure's frequency. Our data suggest that split conformation is an off-pathway state of CtHsp104 during disaggregation. Split conformation of Chaetomium thermophilum Hsp104 disaggregase.,Inoue Y, Hanazono Y, Noi K, Kawamoto A, Kimatsuka M, Harada R, Takeda K, Kita R, Iwamasa N, Shibata K, Noguchi K, Shigeta Y, Namba K, Ogura T, Miki K, Shinohara K, Yohda M Structure. 2021 Feb 25. pii: S0969-2126(21)00046-0. doi:, 10.1016/j.str.2021.02.002. PMID:33651974[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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