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Yorodumi- PDB-12dl: Native structure of the cytoplasmic lattice (CPL) asymmetric unit... -
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Basic information
| Entry | Database: PDB / ID: 12dl | |||||||||||||||||||||||||||
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| Title | Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs | |||||||||||||||||||||||||||
Components |
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Keywords | CYTOSOLIC PROTEIN / cytoplasmic lattice / egg / filamentous assembly | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationregulation of translation by machinery localization / Prolactin receptor signaling / Signaling by BMP / subcortical maternal complex / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / Sealing of the nuclear envelope (NE) by ESCRT-III / establishment of organelle localization / Chromatin modifying enzymes / protein storage ...regulation of translation by machinery localization / Prolactin receptor signaling / Signaling by BMP / subcortical maternal complex / Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Cilium Assembly / Sealing of the nuclear envelope (NE) by ESCRT-III / establishment of organelle localization / Chromatin modifying enzymes / protein storage / structural constituent of cytoplasmic lattice / cytoplasmic lattice / ooplasm / SCF-beta-TrCP mediated degradation of Emi1 / cortical granule exocytosis / embryonic process involved in female pregnancy / endoplasmic reticulum localization / E3 ubiquitin ligases ubiquitinate target proteins / Carboxyterminal post-translational modifications of tubulin / Intraflagellar transport / Downregulation of SMAD2/3:SMAD4 transcriptional activity / establishment or maintenance of apical/basal cell polarity / Regulation of BACH1 activity / COPI-independent Golgi-to-ER retrograde traffic / PINK1-PRKN Mediated Mitophagy / Inactivation of CSF3 (G-CSF) signaling / SCF(Skp2)-mediated degradation of p27/p21 / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MAP3K8 (TPL2)-dependent MAPK1/3 activation / Regulation of TNFR1 signaling / cytoplasm organization / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / histone H3K18 ubiquitin ligase activity / histone H3K14 ubiquitin ligase activity / histone H3 ubiquitin ligase activity / Regulation of RUNX2 expression and activity / Degradation of GLI1 by the proteasome / Cyclin D associated events in G1 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Orc1 removal from chromatin / IKK complex recruitment mediated by RIP1 / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Dectin-1 mediated noncanonical NF-kB signaling / NIK-->noncanonical NF-kB signaling / histone H3K23 ubiquitin ligase activity / COPI-mediated anterograde transport / Aggrephagy / spermatogonial cell division / Kinesins / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / cortical granule / histone H3 reader activity / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / PKR-mediated signaling / Degradation of beta-catenin by the destruction complex / Iron uptake and transport / Activation of NF-kappaB in B cells / The role of GTSE1 in G2/M progression after G2 checkpoint / RHO GTPases activate IQGAPs / FCERI mediated NF-kB activation / Recycling pathway of L1 / CLEC7A (Dectin-1) signaling / COPI-dependent Golgi-to-ER retrograde traffic / Interleukin-1 signaling / apical cortex / positive regulation of meiotic nuclear division / RHO GTPases Activate Formins / chromosomal DNA methylation maintenance following DNA replication / regulation of RNA stability / Separation of Sister Chromatids / positive regulation of embryonic development / Downstream TCR signaling / axonemal microtubule / Hedgehog 'off' state / F-box domain 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 / Peroxisomal protein import / Anchoring of the basal body to the plasma membrane / Recruitment of NuMA to mitotic centrosomes / regulation of establishment of protein localization / AURKA Activation by TPX2 / hemi-methylated DNA-binding / GLI3 is processed to GLI3R by the proteasome / Regulation of PLK1 Activity at G2/M Transition / PcG protein complex / Neddylation / embryonic pattern specification / embryonic cleavage / (E3-independent) E2 ubiquitin-conjugating enzyme / mitochondrion localization / establishment of spindle localization / MHC class II antigen presentation / gap junction / flagellated sperm motility / regulation of epithelial cell proliferation / maintenance of protein location in nucleus Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||||||||||||||||||||
Authors | Li, Y. / Zheng, W. / Leem, J. / Wu, C. / Tang, S. / Mogessie, B. / Xiong, Y. | |||||||||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs Authors: Li, Y. / Zheng, W. / Leem, J. / Wu, C. / Tang, S. / Mogessie, B. / Xiong, Y. | |||||||||||||||||||||||||||
| History |
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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 | 12dl.cif.gz | 2.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb12dl.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 12dl.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/2d/12dl ftp://data.pdbj.org/pub/pdb/validation_reports/2d/12dl | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 76334MC 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
-Protein , 12 types, 27 molecules FAIAJAHBHAKALAMAACADAEAFAGAHAAABAIAJEABABBCACBQBQAQCNA
| #1: Protein | Mass: 49877.824 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||||||||||||||||||
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| #3: Protein | Mass: 18481.295 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 65187.332 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | | Mass: 25512.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | | Mass: 48055.301 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | | Mass: 108001.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 76854.109 Da / Num. of mol.: 10 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | | Mass: 49962.172 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P68373, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement #11: Protein | Mass: 88436.805 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: Q8VDF2, RING-type E3 ubiquitin transferase #12: Protein | Mass: 16706.133 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P61079, E2 ubiquitin-conjugating enzyme, (E3-independent) E2 ubiquitin-conjugating enzyme #14: Protein | Mass: 18693.992 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | | Mass: 54205.703 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-NACHT, LRR and PYD domains-containing protein ... , 2 types, 4 molecules GBGADADB
| #2: Protein | Mass: 131468.547 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 113527.188 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-F-box and WD-40 domain protein ... , 2 types, 2 molecules OAPA
| #13: Protein | Mass: 53657.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #16: Protein | Mass: 54517.043 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 4 types, 16 molecules 






| #17: Chemical | | #18: Chemical | #19: Chemical | ChemComp-ZN / #20: Chemical | ChemComp-CA / | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Native structure of the cytoplasmic lattice (CPL) asymmetric unit from mouse MII eggs Type: COMPLEX / Entity ID: #1-#16 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| Specimen | 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1800 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 249541 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.5 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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