6amn

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Current revision (14:17, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6amn' size='340' side='right'caption='[[6amn]], [[Resolution|resolution]] 2.82&Aring;' scene=''>
<StructureSection load='6amn' size='340' side='right'caption='[[6amn]], [[Resolution|resolution]] 2.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6amn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AMN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6AMN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6amn]] is a 1 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=6AMN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AMN FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6amn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6amn OCA], [http://pdbe.org/6amn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6amn RCSB], [http://www.ebi.ac.uk/pdbsum/6amn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6amn ProSAT]</span></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">X-ray diffraction, [[Resolution|Resolution]] 2.816&#8491;</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=6amn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6amn OCA], [https://pdbe.org/6amn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6amn RCSB], [https://www.ebi.ac.uk/pdbsum/6amn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6amn 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Hsp104 is a ring-forming protein disaggregase that rescues stress-damaged proteins from an aggregated state. To facilitate protein disaggregation, Hsp104 cooperates with Hsp70 and Hsp40 chaperones (Hsp70/40) to form a bi-chaperone system. How Hsp104 recognizes its substrates, particularly the importance of the N domain, remains poorly understood and multiple, seemingly conflicting mechanisms have been proposed. Although the N domain is dispensable for protein disaggregation, it is sensitive to point mutations that abolish the function of the bacterial Hsp104 homolog in vitro, and is essential for curing yeast prions by Hsp104 overexpression in vivo. Here, we present the crystal structure of an N-terminal fragment of Saccharomyces cerevisiae Hsp104 with the N domain of one molecule bound to the C-terminal helix of the neighboring D1 domain. Consistent with mimicking substrate interaction, mutating the putative substrate-binding site in a constitutively active Hsp104 variant impairs the recovery of functional protein from aggregates. We find that the observed substrate-binding defect can be rescued by Hsp70/40 chaperones, providing a molecular explanation as to why the N domain is dispensable for protein disaggregation when Hsp70/40 is present, yet essential for the dissolution of Hsp104-specific substrates, such as yeast prions, which likely depends on a direct N domain interaction.
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Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation.,Lee J, Sung N, Mercado JM, Hryc CF, Chang C, Lee S, Tsai FTF Sci Rep. 2017 Sep 11;7(1):11184. doi: 10.1038/s41598-017-11474-9. PMID:28894176<ref>PMID:28894176</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6amn" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lee, S]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Atpase]]
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[[Category: Lee S]]
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[[Category: Chaperone]]
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Current revision

Crystal Structure of Hsp104 N Domain

PDB ID 6amn

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OCA

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