7OA6
Pseudo-atomic model for Hsp26 residues 63 to 214. Please be advised that the target map is not of sufficient resolution to unambiguously position backbone or side chain atoms. This model represents a likely fit.
Summary for 7OA6
| Entry DOI | 10.2210/pdb7oa6/pdb |
| EMDB information | 12766 12771 12772 12773 |
| Descriptor | Heat shock protein 26 (1 entity in total) |
| Functional Keywords | small heat shock proteins, hsp26 s207e mutant, chaperone |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Total number of polymer chains | 5 |
| Total formula weight | 119552.93 |
| Authors | Muehlhofer, M.,Peters, C.,Kriehuber, T.,Kreuzeder, M.,Kazman, P.,Rodina, N.,Reif, B.,Haslbeck, M.,Weinkauf, S.,Buchner, J. (deposition date: 2021-04-19, release date: 2021-11-24, Last modification date: 2024-07-10) |
| Primary citation | Muhlhofer, M.,Peters, C.,Kriehuber, T.,Kreuzeder, M.,Kazman, P.,Rodina, N.,Reif, B.,Haslbeck, M.,Weinkauf, S.,Buchner, J. Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble. Nat Commun, 12:6697-6697, 2021 Cited by PubMed Abstract: Hsp26 is a small heat shock protein (sHsp) from S. cerevisiae. Its chaperone activity is activated by oligomer dissociation at heat shock temperatures. Hsp26 contains 9 phosphorylation sites in different structural elements. Our analysis of phospho-mimetic mutations shows that phosphorylation activates Hsp26 at permissive temperatures. The cryo-EM structure of the Hsp26 40mer revealed contacts between the conserved core domain of Hsp26 and the so-called thermosensor domain in the N-terminal part of the protein, which are targeted by phosphorylation. Furthermore, several phosphorylation sites in the C-terminal extension, which link subunits within the oligomer, are sensitive to the introduction of negative charges. In all cases, the intrinsic inhibition of chaperone activity is relieved and the N-terminal domain becomes accessible for substrate protein binding. The weakening of domain interactions within and between subunits by phosphorylation to activate the chaperone activity in response to proteotoxic stresses independent of heat stress could be a general regulation principle of sHsps. PubMed: 34795272DOI: 10.1038/s41467-021-27036-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.8 Å) |
Structure validation
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