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- W2480303624 endingPage "837" @default.
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- W2480303624 abstract "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." @default.
- W2480303624 created "2016-08-23" @default.
- W2480303624 creator A5036272439 @default.
- W2480303624 creator A5048244508 @default.
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- W2480303624 date "2016-08-01" @default.
- W2480303624 modified "2023-09-26" @default.
- W2480303624 title "Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation" @default.
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- W2480303624 doi "https://doi.org/10.1038/nsmb.3277" @default.
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- W2480303624 hasPublicationYear "2016" @default.
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