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TitleStructure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism.
Journal, issue, pagesNature, Vol. 601, Issue 7893, Page 465-469, Year 2022
Publish dateDec 22, 2021
AuthorsChari M Noddings / Ray Yu-Ruei Wang / Jill L Johnson / David A Agard /
PubMed AbstractHsp90 is a conserved and essential molecular chaperone responsible for the folding and activation of hundreds of 'client' proteins. The glucocorticoid receptor (GR) is a model client that constantly ...Hsp90 is a conserved and essential molecular chaperone responsible for the folding and activation of hundreds of 'client' proteins. The glucocorticoid receptor (GR) is a model client that constantly depends on Hsp90 for activity. GR ligand binding was previously shown to nr inhibited by Hsp70 and restored by Hsp90, aided by the co-chaperone p23. However, a molecular understanding of the chaperone-mediated remodelling that occurs between the inactive Hsp70-Hsp90 'client-loading complex' and an activated Hsp90-p23 'client-maturation complex' is lacking for any client, including GR. Here we present a cryo-electron microscopy (cryo-EM) structure of the human GR-maturation complex (GR-Hsp90-p23), revealing that the GR ligand-binding domain is restored to a folded, ligand-bound conformation, while being simultaneously threaded through the Hsp90 lumen. In addition, p23 directly stabilizes native GR using a C-terminal helix, resulting in enhanced ligand binding. This structure of a client bound to Hsp90 in a native conformation contrasts sharply with the unfolded kinase-Hsp90 structure. Thus, aided by direct co-chaperone-client interactions, Hsp90 can directly dictate client-specific folding outcomes. Together with the GR-loading complex structure, we present the molecular mechanism of chaperone-mediated GR remodelling, establishing the first, to our knowledge, complete chaperone cycle for any Hsp90 client.
External linksNature / PubMed:34937936 / PubMed Central
MethodsEM (single particle)
Resolution2.56 - 3.63 Å
Structure data

23004

7krj

EMDB-23004, PDB-7krj:
The GR-Maturation Complex: Glucocorticoid Receptor in complex with Hsp90 and co-chaperone p23
Method: EM (single particle) / Resolution: 2.56 Å

EMDB-23005:
Maltose Binding Protein in complex with Hsp90 and co-chaperone p23
Method: EM (single particle) / Resolution: 3.63 Å

EMDB-23006:
Complex of Hsp90 and co-chaperone p23
Method: EM (single particle) / Resolution: 2.66 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-DEX:
DEXAMETHASONE / medication, antibiotic*YM

Source
  • homo sapiens (human)
KeywordsCHAPERONE / ligand binding / ATP binding / protein folding / cryo-EM

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