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Structure paper

TitleMechanisms of assembly and function of the Hsp70-Hsp40 chaperone machinery.
Journal, issue, pagesMol Cell, Vol. 85, Issue 21, Page 4032-44046.e7, Year 2025
Publish dateNov 6, 2025
AuthorsYajun Jiang / Ziad Ibrahim / Youlin Xia / Mary Clay / Alexander Myasnikov / Kalyan Immadisetty / Zhilian Xia / Liang Tang / Paolo Rossi / Pritha Ganguly / Jiangshu Liu / Darcie Miller / Meixia Che / Santiago M Palacios / Günter Kramer / Bernd Bukau / Charalampos G Kalodimos /
PubMed AbstractHsp70 and Hsp40 molecular chaperones form a central machinery that remodels client proteins involved in numerous biological processes. Here, we integrated cryo-electron microscopy and nuclear ...Hsp70 and Hsp40 molecular chaperones form a central machinery that remodels client proteins involved in numerous biological processes. Here, we integrated cryo-electron microscopy and nuclear magnetic resonance spectroscopy to determine the architecture of the full-length Hsp70-Hsp40 machinery. The structure of the complex in a physiologically inhibited state reveals distinct regulatory mechanisms. In the active state, the Hsp40 glycine-phenylalanine (G/F)-rich region acts as a pseudo-substrate for Hsp70, directly modulating refolding. This region also maintains Hsp40 in an autoinhibited state; upon binding to Hsp70, the inhibition is disrupted, exposing a cryptic client-binding site that enables client engagement and refolding. Transitions between these states are central to controlling refolding efficiency. Disrupting either the autoinhibited state or the G/F-Hsp70 interaction impairs function and elicits a compensatory heat shock response in cells. Our findings uncover the regulatory dynamics of a fundamental chaperone system, with broad implications for understanding protein homeostasis and the cellular response to stress.
External linksMol Cell / PubMed:41092901 / PubMed Central
MethodsEM (single particle) / X-ray diffraction / NMR (solution)
Resolution2.75 - 3.37 Å
Structure data

47203

9dvi

EMDB-47203, PDB-9dvi:
Hetero-hexameric Hsp70-Hsp40-DafA complex
Method: EM (single particle) / Resolution: 3.37 Å

PDB-8w1m:
T.thermophilus DNAK nucleotide binding domain in complex with ADP
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

PDB-9dyu:
Assembly and functional mechanisms of the Hsp70-Hsp40 chaperone machinery
Method: SOLUTION NMR

PDB-9dyv:
Assembly and functional mechanisms of the Hsp70-Hsp40 chaperone machinery
Method: SOLUTION NMR

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • thermus thermophilus (bacteria)
KeywordsCHAPERONE / DNAK / Hsp70 / nucleotide binding / ATPase / Hsp40 / protein folding / STRUCTURAL PROTEIN / DnaJ2 and DnaK fusion / DnaJ

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