5VY9
S. cerevisiae Hsp104:casein complex, Middle Domain Conformation
Summary for 5VY9
| Entry DOI | 10.2210/pdb5vy9/pdb |
| Related | 5VJH 5vy8 5vya |
| EMDB information | 8697 8744 8745 8746 |
| Descriptor | Heat shock protein 104, Alpha-S1-casein, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER (3 entities in total) |
| Functional Keywords | hsp104, cryoem, aaa+, chaperone |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 7 |
| Total formula weight | 621723.68 |
| Authors | Gates, S.N.,Yokom, A.L.,Lin, J.-B.,Jackrel, M.E.,Rizo, A.N.,Kendsersky, N.M.,Buell, C.E.,Sweeny, E.A.,Chuang, E.,Torrente, M.P.,Mack, K.L.,Su, M.,Shorter, J.,Southworth, D.R. (deposition date: 2017-05-24, release date: 2017-07-19, Last modification date: 2024-03-13) |
| Primary citation | Gates, S.N.,Yokom, A.L.,Lin, J.,Jackrel, M.E.,Rizo, A.N.,Kendsersky, N.M.,Buell, C.E.,Sweeny, E.A.,Mack, K.L.,Chuang, E.,Torrente, M.P.,Su, M.,Shorter, J.,Southworth, D.R. Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104. Science, 357:273-279, 2017 Cited by PubMed Abstract: 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. PubMed: 28619716DOI: 10.1126/science.aan1052 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.7 Å) |
Structure validation
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