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Open data
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Basic information
| Entry | Database: PDB / ID: 8y0w | ||||||||||||
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| Title | dormant ribosome with eIF5A, eEF2 and SERBP1 | ||||||||||||
Components |
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Keywords | RIBOSOME / dormant ribosome / SERBP1 | ||||||||||||
| Function / homology | Function and homology informationSynthesis of diphthamide-EEF2 / translation at postsynapse / positive regulation of translational termination / Hypusine synthesis from eIF5A-lysine / annulate lamellae / ribosome hibernation / translation elongation factor binding / positive regulation of translational elongation / PML body organization / response to folic acid ...Synthesis of diphthamide-EEF2 / translation at postsynapse / positive regulation of translational termination / Hypusine synthesis from eIF5A-lysine / annulate lamellae / ribosome hibernation / translation elongation factor binding / positive regulation of translational elongation / PML body organization / response to folic acid / SUMO binding / translation at presynapse / exit from mitosis / optic nerve development / positive regulation of cytoplasmic translation / response to insecticide / eukaryotic 80S initiation complex / regulation of translation involved in cellular response to UV / negative regulation of protein neddylation / negative regulation of formation of translation preinitiation complex / axial mesoderm development / regulation of G1 to G0 transition / retinal ganglion cell axon guidance / negative regulation of endoplasmic reticulum unfolded protein response / ribosomal protein import into nucleus / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / positive regulation of respiratory burst involved in inflammatory response / protein-DNA complex disassembly / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / positive regulation of gastrulation / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / protein tyrosine kinase inhibitor activity / positive regulation of endodeoxyribonuclease activity / 90S preribosome assembly / nucleolus organization / IRE1-RACK1-PP2A complex / positive regulation of Golgi to plasma membrane protein transport / aggresome / TNFR1-mediated ceramide production / alpha-beta T cell differentiation / GAIT complex / negative regulation of RNA splicing / negative regulation of DNA repair / positive regulation of DNA damage response, signal transduction by p53 class mediator / TORC2 complex binding / G1 to G0 transition / supercoiled DNA binding / NF-kappaB complex / positive regulation of ubiquitin-protein transferase activity / cysteine-type endopeptidase activator activity involved in apoptotic process / neural crest cell differentiation / oxidized purine DNA binding / middle ear morphogenesis / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / negative regulation of bicellular tight junction assembly / regulation of establishment of cell polarity / ubiquitin-like protein conjugating enzyme binding / rRNA modification in the nucleus and cytosol / erythrocyte homeostasis / negative regulation of phagocytosis / Formation of the ternary complex, and subsequently, the 43S complex / cytoplasmic side of rough endoplasmic reticulum membrane / negative regulation of ubiquitin protein ligase activity / Uptake and function of diphtheria toxin / protein kinase A binding / lncRNA binding / laminin receptor activity / ion channel inhibitor activity / Ribosomal scanning and start codon recognition / homeostatic process / pigmentation / Translation initiation complex formation / positive regulation of mitochondrial depolarization / macrophage chemotaxis / lung morphogenesis / cellular response to actinomycin D / fibroblast growth factor binding / negative regulation of Wnt signaling pathway / positive regulation of T cell receptor signaling pathway / positive regulation of natural killer cell proliferation / male meiosis I / monocyte chemotaxis / negative regulation of translational frameshifting / TOR signaling / BH3 domain binding / Protein hydroxylation / positive regulation of protein binding / positive regulation of activated T cell proliferation / SARS-CoV-1 modulates host translation machinery / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / iron-sulfur cluster binding / mTORC1-mediated signalling / regulation of cell division / Peptide chain elongation / skeletal muscle cell differentiation / cellular response to ethanol / positive regulation of GTPase activity / Selenocysteine synthesis Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||||||||
Authors | Du, M. / Zeng, F. | ||||||||||||
| Funding support | China, 3items
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Citation | Journal: Front Mol Biosci / Year: 2024Title: Implication of Stm1 in the protection of eIF5A, eEF2 and tRNA through dormant ribosomes. Authors: Mengtan Du / Xin Li / Wanlin Dong / Fuxing Zeng / ![]() Abstract: Dormant ribosomes are typically associated with preservation factors to protect themselves from degradation under stress conditions. Stm1/SERBP1 is one such protein that anchors the 40S and 60S ... Dormant ribosomes are typically associated with preservation factors to protect themselves from degradation under stress conditions. Stm1/SERBP1 is one such protein that anchors the 40S and 60S subunits together. Several proteins and tRNAs bind to this complex as well, yet the molecular mechanisms remain unclear. Here, we reported the cryo-EM structures of five newly identified Stm1/SERBP1-bound ribosomes. These structures highlighted that eIF5A, eEF2, and tRNA might bind to dormant ribosomes under stress to avoid their own degradation, thus facilitating protein synthesis upon the restoration of growth conditions. In addition, Ribo-seq data analysis reflected the upregulation of nutrient, metabolism, and external-stimulus-related pathways in the strain, suggesting possible regulatory roles of Stm1. The knowledge generated from the present work will facilitate in better understanding the molecular mechanism of dormant ribosomes. | ||||||||||||
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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 | 8y0w.cif.gz | 4.9 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8y0w.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8y0w.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y0/8y0w ftp://data.pdbj.org/pub/pdb/validation_reports/y0/8y0w | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 37991MC ![]() 8y0uC ![]() 8y0xC 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
-Protein , 5 types, 5 molecules 5CBLmSSg
| #1: Protein | Mass: 16854.264 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P63241 |
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| #2: Protein | Mass: 95463.211 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P13639, Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement |
| #43: Protein | Mass: 14758.394 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62987 |
| #49: Protein | Mass: 44341.781 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q8NC51 |
| #81: Protein | Mass: 35115.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P63244 |
-RNA chain , 4 types, 4 molecules L5L7L8S2
| #3: RNA chain | Mass: 1640222.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 86475748 |
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| #4: RNA chain | Mass: 38998.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 23898 |
| #5: RNA chain | Mass: 50449.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 555853 |
| #50: RNA chain | Mass: 602776.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: 36162 |
+60S ribosomal protein ... , 42 types, 42 molecules LALBLCLDLELFLGLHLILJLLLMLNLOLPLQLRLSLTLULVLWLXLYLZLaLbLcLdLe...
+40S ribosomal protein ... , 30 types, 30 molecules SASBSCSDSESFSGSHSISJSKSLSNSOSPSQSRSSSTSUSVSWSXSYSZSaSbScSdSe
-Non-polymers , 2 types, 231 molecules 


| #82: Chemical | ChemComp-MG / #83: 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: dormant ribosome / Type: RIBOSOME / Details: dormant ribosome with SERBP1, eEF2 and eIF5A / Entity ID: #1-#81 / Source: NATURAL |
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| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 Details: 50mM HEPES, pH7.5, 100mM KOAc, 5mM Mg(OAc)2, 1mM DTT |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Instrument: FEI VITROBOT MARK II / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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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: 2500 nm / Nominal defocus min: 1500 nm |
| Image recording | Electron dose: 30 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: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 74020 / Algorithm: FOURIER SPACE / Symmetry type: POINT | ||||||||||||||||
| Refinement | Cross valid method: NONE |
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About Yorodumi




Homo sapiens (human)
China, 3items
Citation






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FIELD EMISSION GUN