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Structure paper

TitleStructural interplay of the redox co-chaperone CnoX to GroEL/ES chaperonin.
Journal, issue, pagesLife Sci Alliance, Vol. 9, Issue 10, Year 2026
Publish dateAug 7, 2026
AuthorsJunhak Kim / Mingyu Jung / Soung-Hun Roh /
PubMed AbstractProtein folding by the bacterial chaperonin GroEL/ES relies on ATP-driven conformational cycles that promote substrate encapsulation and folding. Under oxidative stress, the redox-active co-chaperone ...Protein folding by the bacterial chaperonin GroEL/ES relies on ATP-driven conformational cycles that promote substrate encapsulation and folding. Under oxidative stress, the redox-active co-chaperone CnoX protects oxidized proteins and associates with GroEL, yet the structural basis of its interaction with the GroEL/ES remains incompletely understood. Using single-particle cryo-electron microscopy, we resolved four distinct nucleotide-bound conformational states of CnoX-associated GroEL/ES complexes. CnoX remains tethered to GroEL through its C-terminal TPR domain despite substantial rearrangements of the GroEL apical domains. We further captured a GroEL/ES-CnoX ternary assembly in which CnoX and GroES simultaneously occupy the same GroEL ring, demonstrating that their binding sites are structurally distinct and non-overlapping. Comparison of two GroES-bound states reveals how apical-domain compaction occludes the CnoX-binding surface and coincides with loss of CnoX from the cis-ring. Together, these structures define how CnoX is accommodated and excluded across distinct GroEL/ES conformations and provide a structural framework for understanding the interplay between redox co-chaperones and chaperonin assemblies.
External linksLife Sci Alliance / PubMed:42567683 / PubMed Central
MethodsEM (single particle)
Resolution2.73 - 3.46 Å
Structure data

65877

9wcw

EMDB-65877, PDB-9wcw:
AMP-PNP bound E.coli CnoX-GroEL complex, state I
Method: EM (single particle) / Resolution: 2.73 Å

EMDB-65953: AMP-PNP bound E.coli CnoX-GroEL complex, state I without symmetry
Method: EM (single particle) / Resolution: 3.11 Å

65990

9wid

EMDB-65990, PDB-9wid:
AMP-PNP bound E.coli CnoX-GroEL complex, state II
Method: EM (single particle) / Resolution: 3.46 Å

65991

9wie

EMDB-65991, PDB-9wie:
AMP-PNP bound E.coli CnoX-GroEL/ES complex, state IV
Method: EM (single particle) / Resolution: 2.79 Å

65992

9wif

EMDB-65992, PDB-9wif:
AMP-PNP bound E.coli CnoX-GroEL/ES complex, state III
Method: EM (single particle) / Resolution: 2.83 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-K:
Unknown entry

Source
  • Escherichia coli K12 (bacteria)
  • escherichia coli k-12 (bacteria)
KeywordsCHAPERONE / Complex

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