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- PDB-8xi3: Structure of mouse SCMC-14-3-3gama complex -

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Basic information

Entry
Database: PDB / ID: 8xi3
TitleStructure of mouse SCMC-14-3-3gama complex
Components
  • 14-3-3 protein gamma
  • NACHT, LRR and PYD domains-containing protein 5
  • Oocyte-expressed protein homolog
  • Transducin-like enhancer protein 6
KeywordsCYTOSOLIC PROTEIN / Complex / Oocyte subcortical / phosphorylation / 14-3-3
Function / homology
Function and homology information


Regulation of localization of FOXO transcription factors / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / RHO GTPases activate PKNs / Activation of BAD and translocation to mitochondria / subcortical maternal complex / establishment of organelle localization / cortical granule exocytosis / endoplasmic reticulum localization / establishment or maintenance of apical/basal cell polarity / ooplasm ...Regulation of localization of FOXO transcription factors / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / RHO GTPases activate PKNs / Activation of BAD and translocation to mitochondria / subcortical maternal complex / establishment of organelle localization / cortical granule exocytosis / endoplasmic reticulum localization / establishment or maintenance of apical/basal cell polarity / ooplasm / TP53 Regulates Metabolic Genes / spermatogonial cell division / cortical granule / positive regulation of embryonic development / positive regulation of meiotic nuclear division / regulation of establishment of protein localization / positive regulation of cell-cell adhesion / regulation of RNA stability / mitochondrion localization / phosphorylation-dependent protein binding / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / apical cortex / Regulation of PLK1 Activity at G2/M Transition / establishment of spindle localization / embryonic pattern specification / positive regulation of T cell mediated immune response to tumor cell / fertilization / regulation of neuron differentiation / positive regulation of neurogenesis / positive regulation of double-strand break repair / exocytosis / replication fork processing / regulation of cell division / positive regulation of double-strand break repair via homologous recombination / protein targeting / cellular response to glucose starvation / negative regulation of TORC1 signaling / insulin-like growth factor receptor binding / embryo implantation / positive regulation of neuron differentiation / protein sequestering activity / protein kinase C binding / actin filament organization / animal organ morphogenesis / regulation of protein stability / regulation of synaptic plasticity / receptor tyrosine kinase binding / positive regulation of T cell activation / cellular response to insulin stimulus / apical part of cell / intracellular protein localization / myelin sheath / presynapse / regulation of protein localization / actin binding / cell cortex / protein-containing complex assembly / vesicle / in utero embryonic development / protein domain specific binding / nucleolus / negative regulation of transcription by RNA polymerase II / Golgi apparatus / protein-containing complex / mitochondrion / RNA binding / ATP binding / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
KH-like RNA-binding domain / : / KH-like RNA-binding domain / Groucho/transducin-like enhancer / : / NACHT, LRR and PYD domains-containing protein, helical domain HD2 / NLRC4 helical domain HD2 / NOD2, winged helix domain / NOD2 winged helix domain / NACHT nucleoside triphosphatase ...KH-like RNA-binding domain / : / KH-like RNA-binding domain / Groucho/transducin-like enhancer / : / NACHT, LRR and PYD domains-containing protein, helical domain HD2 / NLRC4 helical domain HD2 / NOD2, winged helix domain / NOD2 winged helix domain / NACHT nucleoside triphosphatase / NACHT domain / NACHT-NTPase domain profile. / Leucine rich repeat, ribonuclease inhibitor type / Leucine Rich repeat / K Homology domain, type 1 superfamily / 14-3-3 proteins signature 2. / 14-3-3 protein, conserved site / 14-3-3 proteins signature 1. / 14-3-3 protein / 14-3-3 homologues / 14-3-3 domain / 14-3-3 domain superfamily / 14-3-3 protein / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
14-3-3 protein gamma / Oocyte-expressed protein homolog / NACHT, LRR and PYD domains-containing protein 5 / Transducin-like enhancer protein 6
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å
AuthorsChi, P. / Han, Z. / Jiao, H. / Li, J. / Wang, X. / Hu, H. / Deng, D.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31971132 China
CitationJournal: Nat Commun / Year: 2024
Title: The subcortical maternal complex modulates the cell cycle during early mammalian embryogenesis via 14-3-3.
Authors: Zhuo Han / Rui Wang / Pengliang Chi / Zihan Zhang / Ling Min / Haizhan Jiao / Guojin Ou / Dan Zhou / Dandan Qin / Chengpeng Xu / Zheng Gao / Qianqian Qi / Jialu Li / Yuechao Lu / Xiang Wang ...Authors: Zhuo Han / Rui Wang / Pengliang Chi / Zihan Zhang / Ling Min / Haizhan Jiao / Guojin Ou / Dan Zhou / Dandan Qin / Chengpeng Xu / Zheng Gao / Qianqian Qi / Jialu Li / Yuechao Lu / Xiang Wang / Jing Chen / Xingjiang Yu / Hongli Hu / Lei Li / Dong Deng /
Abstract: The subcortical maternal complex (SCMC) is essential for safeguarding female fertility in mammals. Assembled in oocytes, the SCMC maintains the cleavage of early embryos, but the underlying mechanism ...The subcortical maternal complex (SCMC) is essential for safeguarding female fertility in mammals. Assembled in oocytes, the SCMC maintains the cleavage of early embryos, but the underlying mechanism remains unclear. Here, we report that 14-3-3, a multifunctional protein, is a component of the SCMC. By resolving the structure of the 14-3-3-containing SCMC, we discover that phosphorylation of TLE6 contributes to the recruitment of 14-3-3. Mechanistically, during maternal-to-embryo transition, the SCMC stabilizes 14-3-3 protein and contributes to the proper control of CDC25B, thus ensuring the activation of the maturation-promoting factor and mitotic entry in mouse zygotes. Notably, the SCMC establishes a conserved molecular link with 14-3-3 and CDC25B in human oocytes/embryos. This study discloses the molecular mechanism through which the SCMC regulates the cell cycle in early embryos and elucidates the function of the SCMC in mammalian early embryogenesis.
History
DepositionDec 19, 2023Deposition site: PDBJ / Processing site: PDBJ
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
F: 14-3-3 protein gamma
D: 14-3-3 protein gamma
A: NACHT, LRR and PYD domains-containing protein 5
B: Transducin-like enhancer protein 6
C: Oocyte-expressed protein homolog


Theoretical massNumber of molelcules
Total (without water)258,5635
Polymers258,5635
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 14-3-3 protein gamma


Mass: 28336.590 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ywhag
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P61982
#2: Protein NACHT, LRR and PYD domains-containing protein 5 / Maternal antigen that embryos require / Mater protein / Ooplasm-specific protein 1 / OP1


Mass: 119819.859 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Nlrp5, Mater, Nalp5 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9R1M5
#3: Protein Transducin-like enhancer protein 6 / Groucho-related protein 6


Mass: 62304.711 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Tle6, Grg6 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9WVB3
#4: Protein Oocyte-expressed protein homolog / Floped


Mass: 19765.717 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ooep, Oep19 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9CWE6
Has ligand of interestY
Has protein modificationY

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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: mouse SCMC-14-3-3gama complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Mus musculus (house mouse)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 8
SpecimenConc.: 1.8 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN 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: 1200 nm
Image recordingElectron dose: 56.15 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM softwareName: PHENIX / Category: model refinement
CTF correctionType: NONE
3D reconstructionResolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 41406 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00415456
ELECTRON MICROSCOPYf_angle_d0.61720919
ELECTRON MICROSCOPYf_dihedral_angle_d4.1322053
ELECTRON MICROSCOPYf_chiral_restr0.042392
ELECTRON MICROSCOPYf_plane_restr0.0042664

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