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TitleDodecamer assembly of a metazoan AAA chaperone couples substrate extraction to refolding.
Journal, issue, pagesSci Adv, Vol. 9, Issue 19, Page eadf5336, Year 2023
Publish dateMay 10, 2023
AuthorsArpit Gupta / Alfred M Lentzsch / Alex Siegel / Zanlin Yu / Un Seng Chio / Yifan Cheng / Shu-Ou Shan /
PubMed AbstractRing-forming AAA chaperones solubilize protein aggregates and protect organisms from proteostatic stress. In metazoans, the AAA chaperone Skd3 in the mitochondrial intermembrane space (IMS) is ...Ring-forming AAA chaperones solubilize protein aggregates and protect organisms from proteostatic stress. In metazoans, the AAA chaperone Skd3 in the mitochondrial intermembrane space (IMS) is critical for human health and efficiently refolds aggregated proteins, but its underlying mechanism is poorly understood. Here, we show that Skd3 harbors both disaggregase and protein refolding activities enabled by distinct assembly states. High-resolution structures of Skd3 hexamers in distinct conformations capture ratchet-like motions that mediate substrate extraction. Unlike previously described disaggregases, Skd3 hexamers further assemble into dodecameric cages in which solubilized substrate proteins can attain near-native states. Skd3 mutants defective in dodecamer assembly retain disaggregase activity but are impaired in client refolding, linking the disaggregase and refolding activities to the hexameric and dodecameric states of Skd3, respectively. We suggest that Skd3 is a combined disaggregase and foldase, and this property is particularly suited to meet the complex proteostatic demands in the mitochondrial IMS.
External linksSci Adv / PubMed:37163603 / PubMed Central
MethodsEM (single particle)
Resolution2.76 - 6.8 Å
Structure data

26722

7us2

EMDB-26722, PDB-7us2:
PARL-cleaved Skd3 (human ClpB) E455Q Nucleotide Binding Domain hexamer bound to ATPgammaS, open conformation
Method: EM (single particle) / Resolution: 2.76 Å

EMDB-26725: PARL-cleaved Skd3 (human ClpB) E455Q Nucleotide Binding Domain hexamer bound to ATPgammaS, open conformation
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-26726: PARL-cleaved Skd3 (human ClpB) E455Q Nucleotide Binding Domain hexamer bound to ATPgammaS, closed conformation
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-26728: PARL-cleaved Skd3 (human ClpB) E455Q dodecamer bound to ATPgammaS
Method: EM (single particle) / Resolution: 6.8 Å

Chemicals

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsCHAPERONE / AAA+ ATPase / Mitochondria / Protein Folding

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