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- EMDB-34473: Cryo-EM Structure of the CAND1-Cul3-Rbx1 complex -

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Entry
Database: EMDB / ID: EMD-34473
TitleCryo-EM Structure of the CAND1-Cul3-Rbx1 complex
Map data
Sample
  • Complex: CAND1-Cul3-Rbx1 complex
    • Complex: CAND1
      • Protein or peptide: Cullin-associated NEDD8-dissociated protein 1
    • Complex: Cul3, Rbx1
      • Protein or peptide: Cullin-3
      • Protein or peptide: E3 ubiquitin-protein ligase RBX1
  • Ligand: ZINC ION
Keywordsligase / complex
Function / homology
Function and homology information


SCF complex assembly / positive regulation of mitotic cell cycle phase transition / trophectodermal cellular morphogenesis / liver morphogenesis / POZ domain binding / negative regulation of catalytic activity / polar microtubule / nuclear protein quality control by the ubiquitin-proteasome system / COPII vesicle coating / regulation protein catabolic process at postsynapse ...SCF complex assembly / positive regulation of mitotic cell cycle phase transition / trophectodermal cellular morphogenesis / liver morphogenesis / POZ domain binding / negative regulation of catalytic activity / polar microtubule / nuclear protein quality control by the ubiquitin-proteasome system / COPII vesicle coating / regulation protein catabolic process at postsynapse / anaphase-promoting complex-dependent catabolic process / negative regulation of beige fat cell differentiation / RHOBTB3 ATPase cycle / cullin-RING-type E3 NEDD8 transferase / NEDD8 transferase activity / embryonic cleavage / cullin-RING ubiquitin ligase complex / Cul7-RING ubiquitin ligase complex / cellular response to chemical stress / Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling / protein K27-linked ubiquitination / positive regulation of mitotic metaphase/anaphase transition / positive regulation of protein autoubiquitination / RNA polymerase II transcription initiation surveillance / Notch binding / protein neddylation / fibroblast apoptotic process / cell projection organization / NEDD8 ligase activity / negative regulation of Rho protein signal transduction / RHOBTB1 GTPase cycle / negative regulation of response to oxidative stress / VCB complex / Cul5-RING ubiquitin ligase complex / ubiquitin-ubiquitin ligase activity / stem cell division / SCF ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / mitotic metaphase chromosome alignment / negative regulation of type I interferon production / Cul2-RING ubiquitin ligase complex / Cul3-RING ubiquitin ligase complex / stress fiber assembly / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / negative regulation of mitophagy / positive regulation of cytokinesis / Cul4A-RING E3 ubiquitin ligase complex / Cul4-RING E3 ubiquitin ligase complex / Prolactin receptor signaling / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / positive regulation of RNA polymerase II transcription preinitiation complex assembly / cullin family protein binding / endoplasmic reticulum to Golgi vesicle-mediated transport / protein monoubiquitination / ubiquitin ligase complex / RHOBTB2 GTPase cycle / sperm flagellum / site of DNA damage / protein autoubiquitination / protein K48-linked ubiquitination / signal transduction in response to DNA damage / Nuclear events stimulated by ALK signaling in cancer / transcription-coupled nucleotide-excision repair / gastrulation / regulation of cellular response to insulin stimulus / positive regulation of TORC1 signaling / negative regulation of insulin receptor signaling pathway / post-translational protein modification / intrinsic apoptotic signaling pathway / TBP-class protein binding / cyclin binding / positive regulation of protein ubiquitination / Regulation of BACH1 activity / T cell activation / integrin-mediated signaling pathway / negative regulation of canonical NF-kappaB signal transduction / kidney development / cellular response to amino acid stimulus / Degradation of DVL / Degradation of CRY and PER proteins / G1/S transition of mitotic cell cycle / Degradation of GLI1 by the proteasome / negative regulation of canonical Wnt signaling pathway / Iron uptake and transport / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Negative regulation of NOTCH4 signaling / Hedgehog 'on' state / Recognition of DNA damage by PCNA-containing replication complex / Vif-mediated degradation of APOBEC3G / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / RING-type E3 ubiquitin transferase / Degradation of beta-catenin by the destruction complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / DNA Damage Recognition in GG-NER / protein destabilization / NOTCH1 Intracellular Domain Regulates Transcription
Similarity search - Function
TATA-binding protein interacting (TIP20) / Cullin-associated NEDD8-dissociated protein 1/2 / TATA-binding protein interacting (TIP20) / HEAT-like repeat / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / : / Cullin alpha+beta domain / Cullin protein neddylation domain / : ...TATA-binding protein interacting (TIP20) / Cullin-associated NEDD8-dissociated protein 1/2 / TATA-binding protein interacting (TIP20) / HEAT-like repeat / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / : / Cullin alpha+beta domain / Cullin protein neddylation domain / : / Cullin, conserved site / Cullin family signature. / Cullin repeat-like-containing domain superfamily / Cullin protein, neddylation domain / Cullin / Cullin protein neddylation domain / Cullin, N-terminal / Cullin alpha solenoid domain / Cullin / Cullin homology domain / Cullin homology domain superfamily / Cullin family profile. / Zinc finger RING-type profile. / Zinc finger, RING-type / Armadillo-like helical / Armadillo-type fold / Zinc finger, RING/FYVE/PHD-type / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
E3 ubiquitin-protein ligase RBX1 / Cullin-3 / Cullin-associated NEDD8-dissociated protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.76 Å
AuthorsHu Y / Mao Q / Chen Z / Sun L
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)81900729 China
CitationJournal: Nat Struct Mol Biol / Year: 2024
Title: Dynamic molecular architecture and substrate recruitment of cullin3-RING E3 ligase CRL3.
Authors: Yuxia Hu / Zhao Zhang / Qiyu Mao / Xiang Zhang / Aihua Hao / Yu Xun / Yeda Wang / Lin Han / Wuqiang Zhan / Qianying Liu / Yue Yin / Chao Peng / Eva Marie Y Moresco / Zhenguo Chen / Bruce Beutler / Lei Sun /
Abstract: Phosphatidylinositol 3-kinase α, a heterodimer of catalytic p110α and one of five regulatory subunits, mediates insulin- and insulin like growth factor-signaling and, frequently, oncogenesis. ...Phosphatidylinositol 3-kinase α, a heterodimer of catalytic p110α and one of five regulatory subunits, mediates insulin- and insulin like growth factor-signaling and, frequently, oncogenesis. Cellular levels of the regulatory p85α subunit are tightly controlled by regulated proteasomal degradation. In adipose tissue and growth plates, failure of K48-linked p85α ubiquitination causes diabetes, lipodystrophy and dwarfism in mice, as in humans with SHORT syndrome. Here we elucidated the structures of the key ubiquitin ligase complexes regulating p85α availability. Specificity is provided by the substrate receptor KBTBD2, which recruits p85α to the cullin3-RING E3 ubiquitin ligase (CRL3). CRL3 forms multimers, which disassemble into dimers upon substrate binding (CRL3-p85α) and/or neddylation by the activator NEDD8 (CRL3~N8), leading to p85α ubiquitination and degradation. Deactivation involves dissociation of NEDD8 mediated by the COP9 signalosome and displacement of KBTBD2 by the inhibitor CAND1. The hereby identified structural basis of p85α regulation opens the way to better understanding disturbances of glucose regulation, growth and cancer.
History
DepositionOct 9, 2022-
Header (metadata) releaseOct 11, 2023-
Map releaseOct 11, 2023-
UpdateJul 2, 2025-
Current statusJul 2, 2025Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_34473.png

Downloads & links

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Map

FileDownload / File: emd_34473.map.gz / Format: CCP4 / Size: 64 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.)
1.04 Å/pix.
x 256 pix.
= 267.264 Å		1.04 Å/pix.
x 256 pix.
= 267.264 Å		1.04 Å/pix.
x 256 pix.
= 267.264 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.044 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.001
Minimum - Maximum-0.0017580753 - 1.8676628
Average (Standard dev.)0.0020528906 (±0.03332225)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 267.264 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_34473_half_map_1.map
Projections & Slices
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Half map: #1

Fileemd_34473_half_map_2.map
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Sample components

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Entire : CAND1-Cul3-Rbx1 complex

EntireName: CAND1-Cul3-Rbx1 complex
Components
  • Complex: CAND1-Cul3-Rbx1 complex
    • Complex: CAND1
      • Protein or peptide: Cullin-associated NEDD8-dissociated protein 1
    • Complex: Cul3, Rbx1
      • Protein or peptide: Cullin-3
      • Protein or peptide: E3 ubiquitin-protein ligase RBX1
  • Ligand: ZINC ION

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Supramolecule #1: CAND1-Cul3-Rbx1 complex

SupramoleculeName: CAND1-Cul3-Rbx1 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #2: CAND1

SupramoleculeName: CAND1 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1

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Supramolecule #3: Cul3, Rbx1

SupramoleculeName: Cul3, Rbx1 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2-#3

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Macromolecule #1: Cullin-associated NEDD8-dissociated protein 1

MacromoleculeName: Cullin-associated NEDD8-dissociated protein 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 136.529297 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILKLLEDK NGEVQNLAVK CLGPLVSKVK EYQVETIVD TLCTNMLSDK EQLRDISSIG LKTVIGELPP ASSGSALAAN VCKKITGRLT SAIAKQEDVS VQLEALDIMA D MLSRQGGL ...String:
MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILKLLEDK NGEVQNLAVK CLGPLVSKVK EYQVETIVD TLCTNMLSDK EQLRDISSIG LKTVIGELPP ASSGSALAAN VCKKITGRLT SAIAKQEDVS VQLEALDIMA D MLSRQGGL LVNFHPSILT CLLPQLTSPR LAVRKRTIIA LGHLVMSCGN IVFVDLIEHL LSELSKNDSM STTRTYIQCI AA ISRQAGH RIGEYLEKII PLVVKFCNVD DDELREYCIQ AFESFVRRCP KEVYPHVSTI INICLKYLTY DPNYNYDDED EDE NAMDAD GGDDDDQGSD DEYSDDDDMS WKVRRAAAKC LDAVVSTRHE MLPEFYKTVS PALISRFKER EENVKADVFH AYLS LLKQT RPVQSWLCDP DAMEQGETPL TMLQSQVPNI VKALHKQMKE KSVKTRQCCF NMLTELVNVL PGALTQHIPV LVPGI IFSL NDKSSSSNLK IDALSCLYVI LCNHSPQVFH PHVQALVPPV VACVGDPFYK ITSEALLVTQ QLVKVIRPLD QPSSFD ATP YIKDLFTCTI KRLKAADIDQ EVKERAISCM GQIICNLGDN LGSDLPNTLQ IFLERLKNEI TRLTTVKALT LIAGSPL KI DLRPVLGEGV PILASFLRKN QRALKLGTLS ALDILIKNYS DSLTAAMIDA VLDELPPLIS ESDMHVSQMA ISFLTTLA K VYPSSLSKIS GSILNELIGL VRSPLLQGGA LSAMLDFFQA LVVTGTNNLG YMDLLRMLTG PVYSQSTALT HKQSYYSIA KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL SLGEVGHHID LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLP EYLPFVLQEI TSQPKRQYLL LHSLKEIISS ASVVGLKPYV ENIWALLLKH CECAEEGTRN VVAECLGKLT L IDPETLLP RLKGYLISGS SYARSSVVTA VKFTISDHPQ PIDPLLKNCI GDFLKTLEDP DLNVRRVALV TFNSAAHNKP SL IRDLLDT VLPHLYNETK VRKELIREVE MGPFKHTVDD GLDIRKAAFE CMYTLLDSCL DRLDIFEFLN HVEDGLKDHY DIK MLTFLM LVRLSTLCPS AVLQRLDRLV EPLRATCTTK VKANSVKQEF EKQDELKRSA MRAVAALLTI PEAEKSPLMS EFQS QISSN PELAAIFESI QKDSSSTNLE SMDTS

UniProtKB: Cullin-associated NEDD8-dissociated protein 1

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Macromolecule #2: Cullin-3

MacromoleculeName: Cullin-3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 89.063328 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MSNLSKGTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS GLSFEELYRN AYTMVLHKHG EKLYTGLREV VTEHLINKV REDVLNSLNN NFLQTLNQAW NDHQTAMVMI RDILMYMDRV YVQQNNVENV YNLGLIIFRD QVVRYGCIRD H LRQTLLDM ...String:
MSNLSKGTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS GLSFEELYRN AYTMVLHKHG EKLYTGLREV VTEHLINKV REDVLNSLNN NFLQTLNQAW NDHQTAMVMI RDILMYMDRV YVQQNNVENV YNLGLIIFRD QVVRYGCIRD H LRQTLLDM IARERKGEVV DRGAIRNACQ MLMILGLEGR SVYEEDFEAP FLEMSAEFFQ MESQKFLAEN SASVYIKKVE AR INEEIER VMHCLDKSTE EPIVKVVERE LISKHMKTIV EMENSGLVHM LKNGKTEDLG CMYKLFSRVP NGLKTMCECM SSY LREQGK ALVSEEGEGK NPVDYIQGLL DLKSRFDRFL LESFNNDRLF KQTIAGDFEY FLNLNSRSPE YLSLFIDDKL KKGV KGLTE QEVETILDKA MVLFRFMQEK DVFERYYKQH LARRLLTNKS VSDDSEKNMI SKLKTECGCQ FTSKLEGMFR DMSIS NTTM DEFRQHLQAT GVSLGGVDLT VRVLTTGYWP TQSATPKCNI PPAPRHAFEI FRRFYLAKHS GRQLTLQHHM GSADLN ATF YGPVKKEDGS EVGVGGAQVT GSNTRKHILQ VSTFQMTILM LFNNREKYTF EEIQQETDIP ERELVRALQS LACGKPT QR VLTKEPKSKE IENGHIFTVN DQFTSKLHRV KIQTVAAKQG ESDPERKETR QKVDDDRKHE IEAAIVRIMK SRKKMQHN V LVAEVTQQLK ARFLPSPVVI KKRIEGLIER EYLARTPEDR KVYTYVA

UniProtKB: Cullin-3

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Macromolecule #3: E3 ubiquitin-protein ligase RBX1

MacromoleculeName: E3 ubiquitin-protein ligase RBX1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.289977 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ ASATSEECTV AWGVCNHAFH FHCISRWLK TRQVCPLDNR EWEFQKYGH

UniProtKB: E3 ubiquitin-protein ligase RBX1

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Macromolecule #4: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 4 / Number of copies: 3 / Formula: ZN
Molecular weightTheoretical: 65.409 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: 7.8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 53.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

4a0c

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.76 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0) / Number images used: 644994
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING

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