6n8v

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==Hsp104DWB open conformation==
==Hsp104DWB open conformation==
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<StructureSection load='6n8v' size='340' side='right' caption='[[6n8v]], [[Resolution|resolution]] 5.64&Aring;' scene=''>
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<SX load='6n8v' size='340' side='right' viewer='molstar' caption='[[6n8v]], [[Resolution|resolution]] 5.64&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6n8v]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N8V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N8V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6n8v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N8V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.64&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6n8t|6n8t]], [[6n8z|6n8z]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
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<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=6n8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n8v OCA], [http://pdbe.org/6n8v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n8v RCSB], [http://www.ebi.ac.uk/pdbsum/6n8v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n8v ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6n8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n8v OCA], [https://pdbe.org/6n8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n8v RCSB], [https://www.ebi.ac.uk/pdbsum/6n8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n8v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/HS104_YEAST HS104_YEAST]] Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and small Hsps (HSP26), for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by components of the Hsp70/Hsp40 chaperone system. Substrate binding is ATP-dependent, and release of bound polypeptide is triggered by ATP hydrolysis. Also responsible for the maintenance of prions by dissociating prion fibrils into smaller oligomers, thereby producing transmissible seeds that can infect daughter cells during mitosis and meiosis. Loss of HSP104 can cure yeast cells of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].<ref>PMID:10678178</ref> <ref>PMID:11073991</ref> <ref>PMID:11375656</ref> <ref>PMID:11442834</ref> <ref>PMID:12101251</ref> <ref>PMID:14507919</ref> <ref>PMID:15128736</ref> <ref>PMID:15155912</ref> <ref>PMID:15843375</ref> <ref>PMID:15845535</ref> <ref>PMID:1600951</ref> <ref>PMID:16570324</ref> <ref>PMID:16885031</ref> <ref>PMID:17253904</ref> <ref>PMID:17259993</ref> <ref>PMID:17367387</ref> <ref>PMID:17543332</ref> <ref>PMID:18312264</ref> <ref>PMID:2188365</ref> <ref>PMID:7754373</ref> <ref>PMID:7984243</ref> <ref>PMID:8407824</ref> <ref>PMID:8643570</ref> <ref>PMID:9534180</ref> <ref>PMID:9674429</ref>
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[https://www.uniprot.org/uniprot/HS104_YEAST HS104_YEAST] Required, in concert with Hsp40 (YDJ1) and Hsp70 (SSA1) and small Hsps (HSP26), for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by components of the Hsp70/Hsp40 chaperone system. Substrate binding is ATP-dependent, and release of bound polypeptide is triggered by ATP hydrolysis. Also responsible for the maintenance of prions by dissociating prion fibrils into smaller oligomers, thereby producing transmissible seeds that can infect daughter cells during mitosis and meiosis. Loss of HSP104 can cure yeast cells of the prions [PSI+], [URE3] and [PIN+]. Excess HSP104 can also specifically cure cells of [PSI+].<ref>PMID:10678178</ref> <ref>PMID:11073991</ref> <ref>PMID:11375656</ref> <ref>PMID:11442834</ref> <ref>PMID:12101251</ref> <ref>PMID:14507919</ref> <ref>PMID:15128736</ref> <ref>PMID:15155912</ref> <ref>PMID:15843375</ref> <ref>PMID:15845535</ref> <ref>PMID:1600951</ref> <ref>PMID:16570324</ref> <ref>PMID:16885031</ref> <ref>PMID:17253904</ref> <ref>PMID:17259993</ref> <ref>PMID:17367387</ref> <ref>PMID:17543332</ref> <ref>PMID:18312264</ref> <ref>PMID:2188365</ref> <ref>PMID:7754373</ref> <ref>PMID:7984243</ref> <ref>PMID:8407824</ref> <ref>PMID:8643570</ref> <ref>PMID:9534180</ref> <ref>PMID:9674429</ref>
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==See Also==
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*[[Heat Shock Protein structures|Heat Shock Protein structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Lee, J]]
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[[Category: Large Structures]]
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[[Category: Lee, S]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Liu, J]]
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[[Category: Lee J]]
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[[Category: Rho, S H]]
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[[Category: Lee S]]
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[[Category: Sung, N]]
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[[Category: Liu J]]
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[[Category: Tsai, F T.F]]
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[[Category: Rho SH]]
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[[Category: Aaa+]]
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[[Category: Sung N]]
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[[Category: Atpase]]
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[[Category: Tsai FTF]]
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[[Category: Chaperone]]
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[[Category: Clpb]]
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[[Category: Cryo-em]]
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[[Category: Hsp104]]
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[[Category: Molecular chaperone]]
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[[Category: Protein disaggregase]]
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Current revision

Hsp104DWB open conformation

6n8v, resolution 5.64Å

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