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Open data
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Basic information
| Entry | Database: PDB / ID: 8xi3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Title | Structure of mouse SCMC-14-3-3gama complex | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Keywords | CYTOSOLIC PROTEIN / Complex / Oocyte subcortical / phosphorylation / 14-3-3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationRegulation 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 / protein storage / structural constituent of cytoplasmic lattice / cytoplasmic lattice / cortical granule exocytosis ...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 / protein storage / structural constituent of cytoplasmic lattice / cytoplasmic lattice / cortical granule exocytosis / endoplasmic reticulum localization / ooplasm / establishment or maintenance of apical/basal cell polarity / TP53 Regulates Metabolic Genes / spermatogonial cell division / cortical granule / positive regulation of meiotic nuclear division / apical cortex / positive regulation of embryonic development / positive regulation of cell-cell adhesion / regulation of RNA stability / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / regulation of establishment of protein localization / Recruitment of NuMA to mitotic centrosomes / phosphorylation-dependent protein binding / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / mitochondrion localization / Regulation of PLK1 Activity at G2/M Transition / embryonic pattern specification / flagellated sperm motility / positive regulation of T cell mediated immune response to tumor cell / establishment of spindle localization / epigenetic programming in the zygotic pronuclei / fertilization / positive regulation of neurogenesis / regulation of neuron differentiation / positive regulation of double-strand break repair / exocytosis / replication fork processing / regulation of cell division / protein targeting / positive regulation of double-strand break repair via homologous recombination / cellular response to glucose starvation / insulin-like growth factor receptor binding / negative regulation of TORC1 signaling / sperm midpiece / positive regulation of neuron differentiation / embryo implantation / protein kinase C binding / protein sequestering activity / actin filament organization / animal organ morphogenesis / regulation of synaptic plasticity / positive regulation of T cell activation / regulation of protein stability / apical part of cell / intracellular protein localization / myelin sheath / regulation of protein localization / actin binding / protein-containing complex assembly / cell cortex / spermatogenesis / in utero embryonic development / mitochondrial matrix / 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 / cytoplasm / cytosol Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Authors | Chi, P. / Han, Z. / Jiao, H. / Li, J. / Wang, X. / Hu, H. / Deng, D. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: Nat Commun / Year: 2024Title: 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. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8xi3.cif.gz | 353.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8xi3.ent.gz | 277.1 KB | Display | PDB format |
| PDBx/mmJSON format | 8xi3.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8xi3_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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| Full document | 8xi3_full_validation.pdf.gz | 1.5 MB | Display | |
| Data in XML | 8xi3_validation.xml.gz | 64.1 KB | Display | |
| Data in CIF | 8xi3_validation.cif.gz | 97.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xi/8xi3 ftp://data.pdbj.org/pub/pdb/validation_reports/xi/8xi3 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 38369MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 28336.590 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() References: UniProt: P61982 #2: Protein | | Mass: 119819.859 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #3: Protein | | Mass: 62304.711 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #4: Protein | | Mass: 19765.717 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Has ligand of interest | Y | Has protein modification | Y | |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: mouse SCMC-14-3-3gama complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 8 |
| Specimen | Conc.: 1.8 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 56.15 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: NONE | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 41406 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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FIELD EMISSION GUN