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Open data
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Basic information
| Entry | Database: PDB / ID: 7oyd | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Title | Cryo-EM structure of a rabbit 80S ribosome with zebrafish Dap1b | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Keywords | RIBOSOME / translation / embryo / zebrafish / maternal / Dap1 / Dap1b / Habp4 / Eif5a / Eef2b | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationPML body organization / translation elongation factor binding / ribosome hibernation / SUMO binding / regulation of translation involved in cellular response to UV / laminin receptor activity / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / protein-RNA complex assembly / protein-DNA complex disassembly / positive regulation of DNA damage response, signal transduction by p53 class mediator ...PML body organization / translation elongation factor binding / ribosome hibernation / SUMO binding / regulation of translation involved in cellular response to UV / laminin receptor activity / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / protein-RNA complex assembly / protein-DNA complex disassembly / positive regulation of DNA damage response, signal transduction by p53 class mediator / translational elongation / translation elongation factor activity / ubiquitin ligase inhibitor activity / 90S preribosome / positive regulation of signal transduction by p53 class mediator / phagocytic cup / negative regulation of ubiquitin-dependent protein catabolic process / translation regulator activity / ribosomal small subunit export from nucleus / rough endoplasmic reticulum / translation repressor activity / laminin binding / positive regulation of apoptotic signaling pathway / MDM2/MDM4 family protein binding / translation initiation factor binding / apoptotic signaling pathway / negative regulation of autophagy / DNA-(apurinic or apyrimidinic site) lyase / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / ribosomal large subunit biogenesis / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / DNA damage response, signal transduction by p53 class mediator / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / mRNA 3'-UTR binding / positive regulation of translation / small-subunit processome / cellular response to gamma radiation / spindle / mRNA 5'-UTR binding / transcription coactivator binding / rRNA processing / cytosolic ribosome / glucose homeostasis / ribosomal small subunit assembly / ribosome binding / ribosomal small subunit biogenesis / small ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / perikaryon / cytoplasmic translation / protein stabilization / mitochondrial inner membrane / rRNA binding / negative regulation of translation / postsynaptic density / ribonucleoprotein complex / ribosome / translation / structural constituent of ribosome / mRNA binding / ubiquitin protein ligase binding / centrosome / positive regulation of cell population proliferation / nucleolus / dendrite / endoplasmic reticulum membrane / synapse / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / RNA binding / zinc ion binding / nucleoplasm / membrane / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological species | ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.3 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Authors | Leesch, F. / Lorenzo-Orts, L. / Grishkovskaya, I. / Kandolf, S. / Belacic, K. / Meinhart, A. / Haselbach, D. / Pauli, A. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Funding support | Austria, Switzerland, 5items
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Citation | Journal: Nature / Year: 2023Title: A molecular network of conserved factors keeps ribosomes dormant in the egg. Authors: Friederike Leesch / Laura Lorenzo-Orts / Carina Pribitzer / Irina Grishkovskaya / Josef Roehsner / Anastasia Chugunova / Manuel Matzinger / Elisabeth Roitinger / Katarina Belačić / Susanne ...Authors: Friederike Leesch / Laura Lorenzo-Orts / Carina Pribitzer / Irina Grishkovskaya / Josef Roehsner / Anastasia Chugunova / Manuel Matzinger / Elisabeth Roitinger / Katarina Belačić / Susanne Kandolf / Tzi-Yang Lin / Karl Mechtler / Anton Meinhart / David Haselbach / Andrea Pauli / ![]() Abstract: Ribosomes are produced in large quantities during oogenesis and are stored in the egg. However, the egg and early embryo are translationally repressed. Here, using mass spectrometry and cryo-electron ...Ribosomes are produced in large quantities during oogenesis and are stored in the egg. However, the egg and early embryo are translationally repressed. Here, using mass spectrometry and cryo-electron microscopy analyses of ribosomes isolated from zebrafish (Danio rerio) and Xenopus laevis eggs and embryos, we provide molecular evidence that ribosomes transition from a dormant state to an active state during the first hours of embryogenesis. Dormant ribosomes are associated with four conserved factors that form two modules, consisting of Habp4-eEF2 and death associated protein 1b (Dap1b) or Dap in complex with eIF5a. Both modules occupy functionally important sites and act together to stabilize ribosomes and repress translation. Dap1b (also known as Dapl1 in mammals) is a newly discovered translational inhibitor that stably inserts into the polypeptide exit tunnel. Addition of recombinant zebrafish Dap1b protein is sufficient to block translation and reconstitute the dormant egg ribosome state in a mammalian translation extract in vitro. Thus, a developmentally programmed, conserved ribosome state has a key role in ribosome storage and translational repression in the egg. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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 | 7oyd.cif.gz | 4.7 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7oyd.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7oyd.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/oy/7oyd ftp://data.pdbj.org/pub/pdb/validation_reports/oy/7oyd | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 13114MC ![]() 7oyaC ![]() 7oybC ![]() 7oycC 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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| 1 |
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Components
-Ribosomal protein ... , 13 types, 13 molecules xBDDFFNQQQRVWWWYj
| #1: Protein | Mass: 24875.410 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #8: Protein | Mass: 46107.977 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #15: Protein | Mass: 26715.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #21: Protein | Mass: 22913.453 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #36: Protein | Mass: 24207.285 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #42: Protein | Mass: 21699.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #43: Protein | Mass: 16477.377 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #44: Protein | Mass: 23535.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #52: Protein | Mass: 14892.505 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #54: Protein | Mass: 17825.111 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #55: Protein | Mass: 14865.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #58: Protein | Mass: 17303.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #71: Protein | Mass: 11111.032 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-RNA chain , 4 types, 4 molecules 589K
| #2: RNA chain | Mass: 1213395.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #3: RNA chain | Mass: 50157.676 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: RNA chain | Mass: 576826.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #31: RNA chain | Mass: 38691.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
+60S ribosomal protein ... , 34 types, 34 molecules ACDEFGHIJLMOPSTUXZabcdefghikln...
+40S ribosomal protein ... , 25 types, 25 molecules AAAaBBBbCCCcDdEEEeGGHHIIJJLLNNOOPPRRSSTTUUVVXXYYZZ
-Protein , 7 types, 7 molecules GgKKms1tvw
| #24: Protein | Mass: 35115.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #32: Protein | Mass: 18933.846 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #74: Protein | Mass: 14771.411 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #80: Protein | Mass: 12128.150 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #81: Protein | Mass: 16954.340 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #82: Protein | Mass: 95605.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #83: Protein | Mass: 44880.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Non-polymers , 2 types, 208 molecules 


| #84: Chemical | ChemComp-MG / #85: Chemical | ChemComp-ZN / |
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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: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Cryo-EM structure of a rabbit 80S ribosome with zebrafish Dap1b Type: RIBOSOME / Entity ID: #1-#83 / Source: NATURAL | ||||||||||||||||||||||||||||||
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| Molecular weight | Experimental value: NO | ||||||||||||||||||||||||||||||
| Source (natural) | Organism: ![]() | ||||||||||||||||||||||||||||||
| Buffer solution | pH: 7.6 | ||||||||||||||||||||||||||||||
| Buffer component |
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| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
| Specimen support | Grid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R3.5/1 | ||||||||||||||||||||||||||||||
| Vitrification | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 70 % |
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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 / Cs: 2.7 mm / Alignment procedure: ZEMLIN TABLEAU |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 9127 |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 1808120 | ||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 479754 / Details: Composite map of separately refined subunits / Symmetry type: POINT |
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Switzerland, 5items
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FIELD EMISSION GUN