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TitleSpiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 23, Issue 9, Page 830-837, Year 2016
Publish dateAug 1, 2016
AuthorsAdam L Yokom / Stephanie N Gates / Meredith E Jackrel / Korrie L Mack / Min Su / James Shorter / Daniel R Southworth /
PubMed AbstractHsp104, a conserved AAA+ protein disaggregase, promotes survival during cellular stress. Hsp104 remodels amyloids, thereby supporting prion propagation, and disassembles toxic oligomers associated ...Hsp104, a conserved AAA+ protein disaggregase, promotes survival during cellular stress. Hsp104 remodels amyloids, thereby supporting prion propagation, and disassembles toxic oligomers associated with neurodegenerative diseases. However, a definitive structural mechanism for its disaggregase activity has remained elusive. We determined the cryo-EM structure of wild-type Saccharomyces cerevisiae Hsp104 in the ATP state, revealing a near-helical hexamer architecture that coordinates the mechanical power of the 12 AAA+ domains for disaggregation. An unprecedented heteromeric AAA+ interaction defines an asymmetric seam in an apparent catalytic arrangement that aligns the domains in a two-turn spiral. N-terminal domains form a broad channel entrance for substrate engagement and Hsp70 interaction. Middle-domain helices bridge adjacent protomers across the nucleotide pocket, thus explaining roles in ATP hydrolysis and protein disaggregation. Remarkably, substrate-binding pore loops line the channel in a spiral arrangement optimized for substrate transfer across the AAA+ domains, thereby establishing a continuous path for polypeptide translocation.
External linksNat Struct Mol Biol / PubMed:27478928 / PubMed Central
MethodsEM (single particle)
Resolution5.64 Å
Structure data

8267

5kne

EMDB-8267, PDB-5kne:
CryoEM Reconstruction of Hsp104 Hexamer
Method: EM (single particle) / Resolution: 5.64 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCHAPERONE / Hsp104 / AAA+ protein

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