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- EMDB-65991: AMP-PNP bound E.coli CnoX-GroEL/ES complex, state IV -

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Basic information

Entry
Database: EMDB / ID: EMD-65991
TitleAMP-PNP bound E.coli CnoX-GroEL/ES complex, state IV
Map data
Sample
  • Complex: AMP-PNP bound CnoX-GroEL/ES complex
    • Protein or peptide: Chaperonin GroEL
    • Protein or peptide: Co-chaperonin GroES
    • Protein or peptide: Chaperedoxin
  • Ligand: MAGNESIUM ION
  • Ligand: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
  • Ligand: POTASSIUM ION
KeywordsComplex / CHAPERONE
Function / homology
Function and homology information


GroEL-GroES complex / chaperonin ATPase / virion assembly / : / protein folding chaperone / ATP-dependent protein folding chaperone / response to radiation / protein refolding / protein folding / response to heat ...GroEL-GroES complex / chaperonin ATPase / virion assembly / : / protein folding chaperone / ATP-dependent protein folding chaperone / response to radiation / protein refolding / protein folding / response to heat / protein-folding chaperone binding / cellular response to oxidative stress / magnesium ion binding / ATP hydrolysis activity / metal ion binding / ATP binding / membrane / identical protein binding / cytosol
Similarity search - Function
Tetratricopeptide repeat / Chaperonin GroES, conserved site / Chaperonins cpn10 signature. / Chaperonin 10 Kd subunit / GroES chaperonin family / GroES chaperonin superfamily / Chaperonin 10 Kd subunit / Tetratricopeptide repeat / Chaperonin Cpn60, conserved site / Chaperonins cpn60 signature. ...Tetratricopeptide repeat / Chaperonin GroES, conserved site / Chaperonins cpn10 signature. / Chaperonin 10 Kd subunit / GroES chaperonin family / GroES chaperonin superfamily / Chaperonin 10 Kd subunit / Tetratricopeptide repeat / Chaperonin Cpn60, conserved site / Chaperonins cpn60 signature. / Chaperonin Cpn60/GroEL / Thioredoxin / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family / GroES-like superfamily / Thioredoxin domain profile. / Thioredoxin domain / Tetratricopeptide-like helical domain superfamily / Thioredoxin-like superfamily
Similarity search - Domain/homology
Chaperonin GroEL / Co-chaperonin GroES / Chaperedoxin
Similarity search - Component
Biological speciesEscherichia coli K-12 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.79 Å
AuthorsKim J / Roh SH
Funding support Korea, Republic Of, 1 items
OrganizationGrant numberCountry
National Research Foundation (NRF, Korea) Korea, Republic Of
CitationJournal: Life Sci Alliance / Year: 2026
Title: Structural interplay of the redox co-chaperone CnoX to GroEL/ES chaperonin.
Authors: Junhak Kim / Mingyu Jung / Soung-Hun Roh /
Abstract: 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 ...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.
History
DepositionAug 27, 2025-
Header (metadata) releaseAug 5, 2026-
Map releaseAug 5, 2026-
UpdateAug 26, 2026-
Current statusAug 26, 2026Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_65991.png

Downloads & links

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Map

FileDownload / File: emd_65991.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.1 Å/pix.
x 480 pix.
= 528. Å		1.1 Å/pix.
x 480 pix.
= 528. Å		1.1 Å/pix.
x 480 pix.
= 528. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.02
Minimum - Maximum-0.005080031 - 1.9833361
Average (Standard dev.)0.0017781858 (±0.03221196)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 528.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Map before pre-processing

Fileemd_65991_additional_1.map
AnnotationMap before pre-processing
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Half map: #2

Fileemd_65991_half_map_1.map
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Half map: #1

Fileemd_65991_half_map_2.map
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Sample components

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Entire : AMP-PNP bound CnoX-GroEL/ES complex

EntireName: AMP-PNP bound CnoX-GroEL/ES complex
Components
  • Complex: AMP-PNP bound CnoX-GroEL/ES complex
    • Protein or peptide: Chaperonin GroEL
    • Protein or peptide: Co-chaperonin GroES
    • Protein or peptide: Chaperedoxin
  • Ligand: MAGNESIUM ION
  • Ligand: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
  • Ligand: POTASSIUM ION

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Supramolecule #1: AMP-PNP bound CnoX-GroEL/ES complex

SupramoleculeName: AMP-PNP bound CnoX-GroEL/ES complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Escherichia coli K-12 (bacteria)

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Macromolecule #1: Chaperonin GroEL

MacromoleculeName: Chaperonin GroEL / type: protein_or_peptide / ID: 1 / Number of copies: 14 / Enantiomer: LEVO / EC number: chaperonin ATPase
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Molecular weightTheoretical: 57.391711 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGT TTATVLAQAI ITEGLKAVAA GMNPMDLKRG IDKAVTAAVE ELKALSVPCS DSKAIAQVGT ISANSDETVG K LIAEAMDK ...String:
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREI ELEDKFENMG AQMVKEVASK ANDAAGDGT TTATVLAQAI ITEGLKAVAA GMNPMDLKRG IDKAVTAAVE ELKALSVPCS DSKAIAQVGT ISANSDETVG K LIAEAMDK VGKEGVITVE DGTGLQDELD VVEGMQFDRG YLSPYFINKP ETGAVELESP FILLADKKIS NIREMLPVLE AV AKAGKPL LIIAEDVEGE ALATLVVNTM RGIVKVAAVK APGFGDRRKA MLQDIATLTG GTVISEEIGM ELEKATLEDL GQA KRVVIN KDTTTIIDGV GEEAAIQGRV AQIRQQIEEA TSDYDREKLQ ERVAKLAGGV AVIKVGAATE VEMKEKKARV EDAL HATRA AVEEGVVAGG GVALIRVASK LADLRGQNED QNVGIKVALR AMEAPLRQIV LNCGEEPSVV ANTVKGGDGN YGYNA ATEE YGNMIDMGIL DPTKVTRSAL QYAASVAGLM ITTECMVTDL PKNDAADLGA AGGMGGMGGM GGMM

UniProtKB: Chaperonin GroEL

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Macromolecule #2: Co-chaperonin GroES

MacromoleculeName: Co-chaperonin GroES / type: protein_or_peptide / ID: 2 / Number of copies: 7 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Molecular weightTheoretical: 10.400938 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE NGEVKPLDVK VGDIVIFNDG YGVKSEKIDN EEVLIMSES DILAIVEA

UniProtKB: Co-chaperonin GroES

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Macromolecule #3: Chaperedoxin

MacromoleculeName: Chaperedoxin / type: protein_or_peptide / ID: 3 / Number of copies: 7 / Enantiomer: LEVO
Source (natural)Organism: Escherichia coli K-12 (bacteria)
Molecular weightTheoretical: 31.813891 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSVENIVNIN ESNLQQVLEQ SMTTPVLFYF WSERSQHCLQ LTPILESLAA QYNGQFILAK LDCDAEQMIA AQFGLRAIPT VYLFQNGQP VDGFQGPQPE EAIRALLDKV LPREEELKAQ QAMQLMQESN YTDALPLLKD AWQLSNQNGE IGLLLAETLI A LNRSEDAE ...String:
MSVENIVNIN ESNLQQVLEQ SMTTPVLFYF WSERSQHCLQ LTPILESLAA QYNGQFILAK LDCDAEQMIA AQFGLRAIPT VYLFQNGQP VDGFQGPQPE EAIRALLDKV LPREEELKAQ QAMQLMQESN YTDALPLLKD AWQLSNQNGE IGLLLAETLI A LNRSEDAE AVLKTIPLQD QDTRYQGLVA QIELLKQAAD TPEIQQLQQQ VAENPEDAAL ATQLALQLHQ VGRNEEALEL LF GHLRKDL TAADGQTRKT FQEILAALGT GDALASKYRR QLYALLY

UniProtKB: Chaperedoxin

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Macromolecule #4: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 14 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #5: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER

MacromoleculeName: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / type: ligand / ID: 5 / Number of copies: 14 / Formula: ANP
Molecular weightTheoretical: 506.196 Da
Chemical component information

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

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Macromolecule #6: POTASSIUM ION

MacromoleculeName: POTASSIUM ION / type: ligand / ID: 6 / Number of copies: 7 / Formula: K
Molecular weightTheoretical: 39.098 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.8 µm

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Image processing

CTF correctionType: NONE
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

1aon

Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.79 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 133737
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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