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Structure paper

TitleRatchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.
Journal, issue, pagesScience, Vol. 357, Issue 6348, Page 273-279, Year 2017
Publish dateJul 21, 2017
AuthorsStephanie N Gates / Adam L Yokom / JiaBei Lin / Meredith E Jackrel / Alexandrea N Rizo / Nathan M Kendsersky / Courtney E Buell / Elizabeth A Sweeny / Korrie L Mack / Edward Chuang / Mariana P Torrente / Min Su / James Shorter / Daniel R Southworth /
PubMed AbstractHsp100 polypeptide translocases are conserved members of the AAA+ family (adenosine triphosphatases associated with diverse cellular activities) that maintain proteostasis by unfolding aberrant and ...Hsp100 polypeptide translocases are conserved members of the AAA+ family (adenosine triphosphatases associated with diverse cellular activities) that maintain proteostasis by unfolding aberrant and toxic proteins for refolding or proteolytic degradation. The Hsp104 disaggregase from solubilizes stress-induced amorphous aggregates and amyloids. The structural basis for substrate recognition and translocation is unknown. Using a model substrate (casein), we report cryo-electron microscopy structures at near-atomic resolution of Hsp104 in different translocation states. Substrate interactions are mediated by conserved, pore-loop tyrosines that contact an 80-angstrom-long unfolded polypeptide along the axial channel. Two protomers undergo a ratchet-like conformational change that advances pore loop-substrate interactions by two amino acids. These changes are coupled to activation of specific nucleotide hydrolysis sites and, when transmitted around the hexamer, reveal a processive rotary translocation mechanism and substrate-responsive flexibility during Hsp104-catalyzed disaggregation.
External linksScience / PubMed:28619716 / PubMed Central
MethodsEM (single particle)
Resolution4.0 - 6.7 Å
Structure data

8697

5vjh

EMDB-8697, PDB-5vjh:
Closed State CryoEM Reconstruction of Hsp104:ATPyS and FITC casein
Method: EM (single particle) / Resolution: 4.0 Å

8744

5vy8

EMDB-8744, PDB-5vy8:
S. cerevisiae Hsp104-ADP complex
Method: EM (single particle) / Resolution: 5.6 Å

8745

5vy9

EMDB-8745, PDB-5vy9:
S. cerevisiae Hsp104:casein complex, Middle Domain Conformation
Method: EM (single particle) / Resolution: 6.7 Å

8746

5vya

EMDB-8746, PDB-5vya:
S. cerevisiae Hsp104:casein complex, Extended Conformation
Method: EM (single particle) / Resolution: 4.0 Å

Chemicals

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

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • Saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • Bovine (cattle)
  • bos taurus (cattle)
KeywordsCHAPERONE / Hsp104 / cryoem / AAA+

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