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TitleThe structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state.
Journal, issue, pagesMol Cell, Vol. 81, Issue 17, Page 3496-33508.e5, Year 2021
Publish dateSep 2, 2021
AuthorsKanghyun Lee / Aye C Thwin / Cory M Nadel / Eric Tse / Stephanie N Gates / Jason E Gestwicki / Daniel R Southworth /
PubMed AbstractThe Hsp90 chaperone promotes folding and activation of hundreds of client proteins in the cell through an ATP-dependent conformational cycle guided by distinct cochaperone regulators. The FKBP51 ...The Hsp90 chaperone promotes folding and activation of hundreds of client proteins in the cell through an ATP-dependent conformational cycle guided by distinct cochaperone regulators. The FKBP51 immunophilin binds Hsp90 with its tetratricopeptide repeat (TPR) domain and catalyzes peptidyl-prolyl isomerase (PPIase) activity during folding of kinases, nuclear receptors, and tau. Here we determined the cryoelectron microscopy (cryo-EM) structure of the human Hsp90:FKBP51:p23 complex to 3.3 Å, which, together with mutagenesis and crosslinking analyses, reveals the basis for cochaperone binding to Hsp90 during client maturation. A helix extension in the TPR functions as a key recognition element, interacting across the Hsp90 C-terminal dimer interface presented in the closed, ATP conformation. The PPIase domain is positioned along the middle domain, adjacent to Hsp90 client binding sites, whereas a single p23 makes stabilizing interactions with the N-terminal dimer. With this architecture, FKBP51 is positioned to act on specific client residues presented during Hsp90-catalyzed remodeling.
External linksMol Cell / PubMed:34380015 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.3 Å
Structure data

23213

7l7i

EMDB-23213, PDB-7l7i:
Cryo-EM structure of Hsp90:FKBP51:p23 closed-state complex
Method: EM (single particle) / Resolution: 3.3 Å

23214

7l7j

EMDB-23214, PDB-7l7j:
Cryo-EM structure of Hsp90:p23 closed-state complex
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

Source
  • homo sapiens (human)
KeywordsISOMERASE/CHAPERONE / ISOMERASE-CHAPERONE complex / CHAPERONE

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