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| | <StructureSection load='5d4w' size='340' side='right'caption='[[5d4w]], [[Resolution|resolution]] 3.70Å' scene=''> | | <StructureSection load='5d4w' size='340' side='right'caption='[[5d4w]], [[Resolution|resolution]] 3.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5d4w]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_144.50 Cbs 144.50]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D4W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D4W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5d4w]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D4W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5D4W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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]] 3.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0022720 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=209285 CBS 144.50])</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=5d4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d4w OCA], [https://pdbe.org/5d4w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d4w RCSB], [https://www.ebi.ac.uk/pdbsum/5d4w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d4w ProSAT]</span></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=5d4w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d4w OCA], [http://pdbe.org/5d4w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d4w RCSB], [http://www.ebi.ac.uk/pdbsum/5d4w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d4w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G0S4G4_CHATD G0S4G4_CHATD] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5d4w" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5d4w" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Heat Shock Protein structures|Heat Shock Protein structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cbs 144 50]] | + | [[Category: Chaetomium thermophilum]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Clausen, T]] | + | [[Category: Clausen T]] |
| - | [[Category: Heuck, A]] | + | [[Category: Heuck A]] |
| - | [[Category: Schitter-Sollner, S]] | + | [[Category: Schitter-Sollner S]] |
| - | [[Category: Atpase]]
| + | |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Helical filament]]
| + | |
| - | [[Category: Protein disaggregase]]
| + | |
| - | [[Category: Two-ring aaa protein]]
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| Structural highlights
Function
G0S4G4_CHATD
Publication Abstract from PubMed
The Hsp104 disaggregase is a two-ring ATPase machine that rescues various forms of non-native proteins including the highly resistant amyloid fibers. The structural-mechanistic underpinnings of how the recovery of toxic protein aggregates is promoted and how this potent unfolding activity is prevented from doing collateral damage to cellular proteins are not well understood. Here, we present structural and biochemical data revealing the organization of Hsp104 from Chaetomium thermophilum at 3.7 A resolution. We show that the coiled-coil domains encircling the disaggregase constitute a 'restraint mask' that sterically controls the mobility and thus the unfolding activity of the ATPase modules. In addition, we identify a mechanical linkage that coordinates the activity of the two ATPase rings and accounts for the high unfolding potential of Hsp104. Based on these findings, we propose a general model for how Hsp104 and related chaperones operate and are kept under control until recruited to appropriate substrates.
Structural basis for the disaggregase activity and regulation of Hsp104.,Heuck A, Schitter-Sollner S, Suskiewicz MJ, Kurzbauer R, Kley J, Schleiffer A, Rombaut P, Herzog F, Clausen T Elife. 2016 Nov 30;5. pii: e21516. doi: 10.7554/eLife.21516. PMID:27901467[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Heuck A, Schitter-Sollner S, Suskiewicz MJ, Kurzbauer R, Kley J, Schleiffer A, Rombaut P, Herzog F, Clausen T. Structural basis for the disaggregase activity and regulation of Hsp104. Elife. 2016 Nov 30;5. pii: e21516. doi: 10.7554/eLife.21516. PMID:27901467 doi:http://dx.doi.org/10.7554/eLife.21516
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