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- PDB-9lpk: Structure of human PADI6-UHRF1-UBE2D3 complex -

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Basic information

Entry
Database: PDB / ID: 9lpk
TitleStructure of human PADI6-UHRF1-UBE2D3 complex
Components
  • E3 ubiquitin-protein ligase UHRF1
  • Protein-arginine deiminase type-6
  • Ubiquitin-conjugating enzyme E2 D3
KeywordsLIGASE/HYDROLASE / PADI6 / UHRF1 / UBE2D3 / ubiquitylation / maternal complex / early embryonic development / LIGASE-HYDROLASE complex
Function / homology
Function and homology information


regulation of translation by machinery localization / protein storage / structural constituent of cytoplasmic lattice / cytoplasmic lattice / cytoplasm organization / histone H3K18 ubiquitin ligase activity / histone H3K14 ubiquitin ligase activity / histone H3 ubiquitin ligase activity / histone H3K23 ubiquitin ligase activity / cortical granule ...regulation of translation by machinery localization / protein storage / structural constituent of cytoplasmic lattice / cytoplasmic lattice / cytoplasm organization / histone H3K18 ubiquitin ligase activity / histone H3K14 ubiquitin ligase activity / histone H3 ubiquitin ligase activity / histone H3K23 ubiquitin ligase activity / cortical granule / chromosomal DNA methylation maintenance following DNA replication / DNA damage sensor activity / hemi-methylated DNA-binding / homologous recombination / Signaling by BMP / embryonic cleavage / (E3-independent) E2 ubiquitin-conjugating enzyme / regulation of epithelial cell proliferation / intermediate filament cytoskeleton / methyl-CpG binding / protein K11-linked ubiquitination / protein K6-linked ubiquitination / epigenetic programming in the zygotic pronuclei / histone H3K9me2/3 reader activity / : / E2 ubiquitin-conjugating enzyme / negative regulation of gene expression via chromosomal CpG island methylation / positive regulation of protein metabolic process / ubiquitin conjugating enzyme activity / mitotic spindle assembly / negative regulation of BMP signaling pathway / protein monoubiquitination / protein autoubiquitination / cis-regulatory region sequence-specific DNA binding / Chromatin modifying enzymes / heterochromatin / protein localization to chromatin / protein K48-linked ubiquitination / cytoskeleton organization / epigenetic regulation of gene expression / TICAM1, RIP1-mediated IKK complex recruitment / protein modification process / replication fork / DNA methylation / Chromatin modifications during the maternal to zygotic transition (MZT) / IKK complex recruitment mediated by RIP1 / PINK1-PRKN Mediated Mitophagy / Negative regulators of DDX58/IFIH1 signaling / Peroxisomal protein import / Downregulation of SMAD2/3:SMAD4 transcriptional activity / Regulation of TNFR1 signaling / tubulin binding / euchromatin / RING-type E3 ubiquitin transferase / Inactivation of CSF3 (G-CSF) signaling / double-strand break repair via homologous recombination / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / spindle / nuclear matrix / protein polyubiquitination / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / Antigen processing: Ubiquitination & Proteasome degradation / heterochromatin formation / E3 ubiquitin ligases ubiquitinate target proteins / Neddylation / histone binding / ubiquitin-dependent protein catabolic process / nucleic acid binding / in utero embryonic development / proteasome-mediated ubiquitin-dependent protein catabolic process / endosome membrane / protein ubiquitination / DNA repair / apoptotic process / calcium ion binding / DNA damage response / chromatin / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / extracellular exosome / zinc ion binding / nucleoplasm / ATP binding / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
: / UHRF1, tandem tudor domain / Tandem tudor domain within UHRF1 / UHRF1/2-like / Protein-arginine deiminase / Protein-arginine deiminase, C-terminal / Protein-arginine deiminase (PAD), N-terminal / Protein-arginine deiminase (PAD), central domain / Protein-arginine deiminase, central domain superfamily / PAD, N-terminal domain superfamily ...: / UHRF1, tandem tudor domain / Tandem tudor domain within UHRF1 / UHRF1/2-like / Protein-arginine deiminase / Protein-arginine deiminase, C-terminal / Protein-arginine deiminase (PAD), N-terminal / Protein-arginine deiminase (PAD), central domain / Protein-arginine deiminase, central domain superfamily / PAD, N-terminal domain superfamily / Protein-arginine deiminase (PAD) / Protein-arginine deiminase (PAD) N-terminal domain / Protein-arginine deiminase (PAD) middle domain / SRA-YDG / SRA-YDG superfamily / SAD/SRA domain / YDG domain profile. / SET and RING finger associated domain. Domain of unknown function in SET domain containing proteins and in Deinococcus radiodurans DRA1533. / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / PUA-like superfamily / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme/RWD-like / PHD-finger / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Zinc finger PHD-type signature. / Ring finger / Cupredoxin / Zinc finger PHD-type profile. / Zinc finger, PHD-finger / Zinc finger, PHD-type / PHD zinc finger / Zinc finger, FYVE/PHD-type / Zinc finger RING-type profile. / Zinc finger, RING-type / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Zinc finger, RING/FYVE/PHD-type / Ubiquitin-like domain superfamily
Similarity search - Domain/homology
Ubiquitin-conjugating enzyme E2 D3 / Inactive protein-arginine deiminase type-6 / E3 ubiquitin-protein ligase UHRF1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.03 Å
AuthorsLi, J. / Deng, D.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31871449 China
CitationJournal: Nat Struct Mol Biol / Year: 2026
Title: The maternal PADI6-UHRF1-UBE2D complex regulates ubiquitination during oocyte maturation and embryogenesis.
Authors: Jinhong Li / Yuechao Lu / Zhili Xia / Pengliang Chi / Qianqian Qi / Sibei Liu / Sicheng Ju / Jialu Li / Zihan Zhang / Zhuo Han / Qingting Liu / Wenbo Meng / Jing Chen / Xiang Wang / Li Guo / ...Authors: Jinhong Li / Yuechao Lu / Zhili Xia / Pengliang Chi / Qianqian Qi / Sibei Liu / Sicheng Ju / Jialu Li / Zihan Zhang / Zhuo Han / Qingting Liu / Wenbo Meng / Jing Chen / Xiang Wang / Li Guo / Lei Li / Wei Huang / Lunzhi Dai / Junhong Han / Shaorong Gao / Dong Deng /
Abstract: Proteostasis in mammalian oocytes is vital for successful reproduction. The cytoplasmic lattices (CPLs) of oocytes store essential maternal proteins for early embryo development. Here we show that ...Proteostasis in mammalian oocytes is vital for successful reproduction. The cytoplasmic lattices (CPLs) of oocytes store essential maternal proteins for early embryo development. Here we show that PADI6, a core component of CPLs, forms a conserved ternary complex that we term MPU for maternal PADI6-UHRF1-UBE2D. The MPU complex regulates protein ubiquitination during oocyte maturation and early embryogenesis. We determined the cryo-electron microscopy structure of MPU and show that 86% (25/29) of clinically identified PADI6 missense variants disrupt MPU assembly, revealing a potential molecular mechanism linking dysregulation of ubiquitination on oocytes to abnormal embryonic development. Mechanistically, PADI6, with the assistance of UHRF1, sequesters UBE2D to prevent ubiquitin transfer from E2 to relevant substrate proteins, thereby suppressing the ubiquitination cascade. Therefore, our findings implicate PADI6 in the regulation of proteostasis by controlling the ubiquitination cascade, expanding our understanding of PADI6-dependent regulation of oocyte maturation and early embryogenesis.
History
DepositionJan 25, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Jan 28, 2026Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: E3 ubiquitin-protein ligase UHRF1
C: Protein-arginine deiminase type-6
B: Protein-arginine deiminase type-6
E: Ubiquitin-conjugating enzyme E2 D3
D: Ubiquitin-conjugating enzyme E2 D3
F: E3 ubiquitin-protein ligase UHRF1


Theoretical massNumber of molelcules
Total (without water)368,9216
Polymers368,9216
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein E3 ubiquitin-protein ligase UHRF1 / Inverted CCAAT box-binding protein of 90 kDa / Nuclear protein 95 / Nuclear zinc finger protein ...Inverted CCAAT box-binding protein of 90 kDa / Nuclear protein 95 / Nuclear zinc finger protein Np95 / HuNp95 / hNp95 / RING finger protein 106 / RING-type E3 ubiquitin transferase UHRF1 / Transcription factor ICBP90 / Ubiquitin-like PHD and RING finger domain-containing protein 1 / hUHRF1 / Ubiquitin-like-containing PHD and RING finger domains protein 1


Mass: 89948.078 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UHRF1, ICBP90, NP95, RNF106 / Cell line (production host): HEK293F / Production host: Homo sapiens (human)
References: UniProt: Q96T88, RING-type E3 ubiquitin transferase
#2: Protein Protein-arginine deiminase type-6 / Peptidyl arginine deiminase-like protein / Peptidylarginine deiminase VI / hPADVI / Protein- ...Peptidyl arginine deiminase-like protein / Peptidylarginine deiminase VI / hPADVI / Protein-arginine deiminase type VI


Mass: 77806.141 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PADI6, PAD6 / Cell (production host): HEK293F / Cell line (production host): HEK293F / Production host: Homo sapiens (human) / References: UniProt: Q6TGC4, protein-arginine deiminase
#3: Protein Ubiquitin-conjugating enzyme E2 D3 / (E3-independent) E2 ubiquitin-conjugating enzyme D3 / E2 ubiquitin-conjugating enzyme D3 / ...(E3-independent) E2 ubiquitin-conjugating enzyme D3 / E2 ubiquitin-conjugating enzyme D3 / Ubiquitin carrier protein D3 / Ubiquitin-conjugating enzyme E2(17)KB 3 / Ubiquitin-conjugating enzyme E2-17 kDa 3 / Ubiquitin-protein ligase D3


Mass: 16706.133 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2D3, UBC5C, UBCH5C / Cell line (production host): HEK293F / Production host: Homo sapiens (human)
References: UniProt: P61077, E2 ubiquitin-conjugating enzyme, (E3-independent) E2 ubiquitin-conjugating enzyme
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Heterohexamer of human PADI6-UHRF1-UBE2D3 complex / Type: COMPLEX / Entity ID: all / Source: MULTIPLE SOURCES
Molecular weightExperimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Homo sapiens (human)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: OTHER

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 1100 nm
Image recordingElectron dose: 55.13 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

EM softwareName: PHENIX / Version: 1.20.1_4487 / Category: model refinement
CTF correctionType: NONE
3D reconstructionResolution: 3.03 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 31091 / Symmetry type: POINT
RefinementHighest resolution: 3.03 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00416678
ELECTRON MICROSCOPYf_angle_d0.56122648
ELECTRON MICROSCOPYf_dihedral_angle_d3.4472235
ELECTRON MICROSCOPYf_chiral_restr0.0432481
ELECTRON MICROSCOPYf_plane_restr0.0052933

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