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Open data
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Basic information
| Entry | Database: PDB / ID: 8fl3 | |||||||||
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| Title | Human nuclear pre-60S ribosomal subunit (State I2) | |||||||||
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Keywords | RIBOSOME / Pre-60S ribosomal subunit / Assembly intermediate / Nucleoprotein complex | |||||||||
| Function / homology | Function and homology informationmitotic nuclear division / rixosome complex / protein localization to nucleoplasm / Las1 complex / negative regulation of transcription of nucleolar large rRNA by RNA polymerase I / negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding / positive regulation of protein localization to chromosome, telomeric region / regulation of RIG-I signaling pathway / : / dendrite extension ...mitotic nuclear division / rixosome complex / protein localization to nucleoplasm / Las1 complex / negative regulation of transcription of nucleolar large rRNA by RNA polymerase I / negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding / positive regulation of protein localization to chromosome, telomeric region / regulation of RIG-I signaling pathway / : / dendrite extension / inner cell mass cell differentiation / hematopoietic stem cell homeostasis / preribosome binding / lamin filament / regulation of Notch signaling pathway / regulation of megakaryocyte differentiation / PTK6 Expression / regulation of fatty acid biosynthetic process / miRNA-mediated post-transcriptional gene silencing / dynein axonemal particle / PeBoW complex / negative regulation of G2/M transition of mitotic cell cycle / positive regulation of protein sumoylation / SUMO binding / miRNA-mediated gene silencing by inhibition of translation / nuclear pre-replicative complex / translation at presynapse / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / positive regulation of protein K63-linked deubiquitination / blastocyst formation / protein localization to nucleolus / negative regulation of mitotic cell cycle / regulation of translation involved in cellular response to UV / eukaryotic 80S initiation complex / negative regulation of formation of translation preinitiation complex / axial mesoderm development / ribosomal protein import into nucleus / regulation of G1 to G0 transition / protein-DNA complex disassembly / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / 90S preribosome assembly / alpha-beta T cell differentiation / regulation of glycolytic process / skeletal system morphogenesis / positive regulation of DNA damage response, signal transduction by p53 class mediator / GAIT complex / negative regulation of cell-cell adhesion / TORC2 complex binding / regulation of reactive oxygen species metabolic process / maturation of 5.8S rRNA / stem cell division / G1 to G0 transition / regulation of aerobic respiration / middle ear morphogenesis / cytoplasmic side of rough endoplasmic reticulum membrane / stem cell population maintenance / rRNA metabolic process / regulation of protein phosphorylation / negative regulation of DNA replication / mitotic G2 DNA damage checkpoint signaling / positive regulation of dendritic spine development / ribosomal large subunit binding / homeostatic process / preribosome, large subunit precursor / macrophage chemotaxis / negative regulation of signal transduction by p53 class mediator / lung morphogenesis / positive regulation of telomere maintenance / positive regulation of natural killer cell proliferation / MLL1 complex / rRNA transcription / Protein hydroxylation / cellular response to estrogen stimulus / nuclear-transcribed mRNA catabolic process / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / ribosomal large subunit export from nucleus / Eukaryotic Translation Termination / blastocyst development / ubiquitin ligase inhibitor activity / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / Viral mRNA Translation / ribonucleoprotein complex binding / positive regulation of signal transduction by p53 class mediator / protein localization to nucleus / negative regulation of ubiquitin-dependent protein catabolic process / somitogenesis / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / ribosomal subunit export from nucleus / L13a-mediated translational silencing of Ceruloplasmin expression / negative regulation of protein-containing complex assembly / protein targeting / Major pathway of rRNA processing in the nucleolus and cytosol / protein-RNA complex assembly / maturation of LSU-rRNA / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Notch signaling pathway Similarity search - Function | |||||||||
| Biological species | Homo sapiens (human) | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.53 Å | |||||||||
Authors | Vanden Broeck, A. / Klinge, S. | |||||||||
| Funding support | European Union, United States, 2items
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Citation | Journal: Science / Year: 2023Title: Principles of human pre-60 biogenesis. Authors: Arnaud Vanden Broeck / Sebastian Klinge / ![]() Abstract: During the early stages of human large ribosomal subunit (60) biogenesis, an ensemble of assembly factors establishes and fine-tunes the essential RNA functional centers of pre-60 particles by an ...During the early stages of human large ribosomal subunit (60) biogenesis, an ensemble of assembly factors establishes and fine-tunes the essential RNA functional centers of pre-60 particles by an unknown mechanism. Here, we report a series of cryo-electron microscopy structures of human nucleolar and nuclear pre-60 assembly intermediates at resolutions of 2.5 to 3.2 angstroms. These structures show how protein interaction hubs tether assembly factor complexes to nucleolar particles and how guanosine triphosphatases and adenosine triphosphatase couple irreversible nucleotide hydrolysis steps to the installation of functional centers. Nuclear stages highlight how a conserved RNA-processing complex, the rixosome, couples large-scale RNA conformational changes with pre-ribosomal RNA processing by the RNA degradation machinery. Our ensemble of human pre-60 particles provides a rich foundation with which to elucidate the molecular principles of ribosome formation. | |||||||||
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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 | 8fl3.cif.gz | 4.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8fl3.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8fl3.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fl/8fl3 ftp://data.pdbj.org/pub/pdb/validation_reports/fl/8fl3 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 29266MC ![]() 8fkpC ![]() 8fkqC ![]() 8fkrC ![]() 8fksC ![]() 8fktC ![]() 8fkuC ![]() 8fkvC ![]() 8fkwC ![]() 8fkxC ![]() 8fkyC ![]() 8fkzC ![]() 8fl0C ![]() 8fl2C ![]() 8fl4C ![]() 8fl6C ![]() 8fl7C ![]() 8fl9C ![]() 8flaC ![]() 8flbC ![]() 8flcC ![]() 8fldC ![]() 8fleC ![]() 8flfC C: citing same article ( M: map data used to model this data |
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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
+60S ribosomal protein ... , 39 types, 39 molecules BABBL5L6L7L8L9LALBLCLDLELFLGLHLILJLKLLLNLOLPLQLRLSLTLULWLXLY...
-Protein , 17 types, 19 molecules BDNBNCNJNKNPNTNUNVNWNXNYNZSHSKSMSQSRSV
| #3: Protein | Mass: 83153.734 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9Y4W2 | ||||||||||||||||
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| #36: Protein | Mass: 62098.242 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9BVP2 | ||||||||||||||||
| #37: Protein | Mass: 83796.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q13823 | ||||||||||||||||
| #39: Protein | Mass: 53387.141 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9NVX2 | ||||||||||||||||
| #40: Protein | Mass: 15268.361 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9BRT6 | ||||||||||||||||
| #42: Protein | Mass: 15230.225 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: O00488 | ||||||||||||||||
| #43: Protein | Mass: 80005.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9NVU7 | ||||||||||||||||
| #44: Protein | Mass: 105811.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9NXF1 | ||||||||||||||||
| #45: Protein | Mass: 47459.121 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9BV38#46: Protein | Mass: 119786.648 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q8IZL8#47: Protein | | Mass: 40312.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9H6F5#55: Protein | | Mass: 34285.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9BYG3#57: Protein | | Mass: 26620.010 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: P56537#58: Protein | | Mass: 68114.727 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: O00541#59: Protein | | Mass: 27602.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9UKD2#60: Protein | | Mass: 74107.820 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9BZE4#61: Protein | | Mass: 19666.258 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9UHA3 |
-RNA chain , 3 types, 3 molecules L1L3L4
| #4: RNA chain | Mass: 50463.840 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: GenBank: 555853 |
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| #5: RNA chain | Mass: 1641203.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: GenBank: 86475748 |
| #6: RNA chain | Mass: 38998.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: GenBank: 23898 |
-Ribosome biogenesis protein ... , 2 types, 2 molecules NFNL
| #38: Protein | Mass: 30136.703 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: O95478 |
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| #41: Protein | Mass: 54498.402 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293F / References: UniProt: Q9NZM5 |
-Non-polymers , 5 types, 109 molecules 








| #62: Chemical | ChemComp-MG / #63: Chemical | ChemComp-ZN / #64: Chemical | ChemComp-GTP / | #65: Chemical | #66: Chemical | ChemComp-GDP / | |
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-Details
| Has ligand of interest | N |
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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: Human nuclear pre-60S ribosomal subunit (State I2) / Type: RIBOSOME / Entity ID: #1-#61 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) / Strain: HEK293F |
| Buffer solution | pH: 7.6 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: GOLD / Grid mesh size: 400 divisions/in. / Grid type: Quantifoil R3.5/1 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 283 K Details: Four applications with manual blotting before last blotting with the vitrobot. |
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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 magnification: 64000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm |
| Image recording | Average exposure time: 2 sec. / Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 4 / Num. of real images: 172699 |
| EM imaging optics | Energyfilter slit width: 20 eV |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 15679142 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.53 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 107973 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||||||||||||
| Atomic model building | Space: REAL |
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About Yorodumi




Homo sapiens (human)
United States, 2items
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