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Open data
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Basic information
| Entry | Database: PDB / ID: 8ir1 | |||||||||||||||||||||||||||||||||
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| Title | human nuclear pre-60S ribosomal particle - State A | |||||||||||||||||||||||||||||||||
Components |
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Keywords | RIBOSOME / GNL2 / nuclear / pre-60S | |||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationRNA 2'-O-methyltransferase activity / positive regulation of protein localization to chromosome, telomeric region / basal RNA polymerase II transcription machinery binding / rRNA (uridine-2'-O-)-methyltransferase activity / dendrite extension / rRNA (guanine) methyltransferase activity / inner cell mass cell differentiation / preribosome binding / hematopoietic stem cell homeostasis / lamin filament ...RNA 2'-O-methyltransferase activity / positive regulation of protein localization to chromosome, telomeric region / basal RNA polymerase II transcription machinery binding / rRNA (uridine-2'-O-)-methyltransferase activity / dendrite extension / rRNA (guanine) methyltransferase activity / inner cell mass cell differentiation / preribosome binding / hematopoietic stem cell homeostasis / lamin filament / regulation of fatty acid biosynthetic process / RNA methylation / regulation of Notch signaling pathway / regulation of megakaryocyte differentiation / miRNA-mediated post-transcriptional gene silencing / negative regulation of G2/M transition of mitotic cell cycle / positive regulation of protein sumoylation / miRNA-mediated gene silencing by inhibition of translation / translation at presynapse / eukaryotic 80S initiation complex / negative regulation of protein neddylation / regulation of translation involved in cellular response to UV / axial mesoderm development / negative regulation of formation of translation preinitiation complex / regulation of G1 to G0 transition / ribosomal protein import into nucleus / protein-DNA complex disassembly / maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / 90S preribosome assembly / protein localization to nucleolus / negative regulation of mitotic cell cycle / GAIT complex / positive regulation of DNA damage response, signal transduction by p53 class mediator / rRNA methylation / TORC2 complex binding / alpha-beta T cell differentiation / G1 to G0 transition / regulation of glycolytic process / middle ear morphogenesis / skeletal system morphogenesis / regulation of reactive oxygen species metabolic process / negative regulation of cell-cell adhesion / cytoplasmic side of rough endoplasmic reticulum membrane / stem cell division / maturation of 5.8S rRNA / negative regulation of ubiquitin protein ligase activity / mitotic metaphase chromosome alignment / preribosome, small subunit precursor / stem cell population maintenance / homeostatic process / negative regulation of DNA replication / positive regulation of dendritic spine development / macrophage chemotaxis / lung morphogenesis / positive regulation of telomere maintenance / ribosomal large subunit binding / positive regulation of natural killer cell proliferation / Protein hydroxylation / preribosome, large subunit precursor / Peptide chain elongation / nuclear-transcribed mRNA catabolic process / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / ubiquitin ligase inhibitor activity / cellular response to actinomycin D / Response of EIF2AK4 (GCN2) to amino acid deficiency / blastocyst development / SRP-dependent cotranslational protein targeting to membrane / negative regulation of ubiquitin-dependent protein catabolic process / positive regulation of signal transduction by p53 class mediator / Viral mRNA Translation / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / protein localization to nucleus / L13a-mediated translational silencing of Ceruloplasmin expression / positive regulation of protein binding / Major pathway of rRNA processing in the nucleolus and cytosol / somitogenesis / hematopoietic progenitor cell differentiation / protein targeting / protein-RNA complex assembly / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / ribosomal subunit export from nucleus / maturation of LSU-rRNA / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / rough endoplasmic reticulum / Notch signaling pathway / MDM2/MDM4 family protein binding / translation initiation factor activity / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / negative regulation of protein ubiquitination / cytosolic ribosome / cellular response to interleukin-4 / ossification / negative regulation of cell migration / assembly of large subunit precursor of preribosome / Transferases; Transferring one-carbon groups; Methyltransferases / positive regulation of translation Similarity search - Function | |||||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||||||||||||||||||||||||||
Authors | Zhang, Y. / Gao, N. | |||||||||||||||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: Cell Res / Year: 2023Title: Visualizing the nucleoplasmic maturation of human pre-60S ribosomal particles. Authors: Yunyang Zhang / Xiaomeng Liang / Sha Luo / Yan Chen / Yu Li / Chengying Ma / Ningning Li / Ning Gao / ![]() Abstract: Eukaryotic ribosome assembly is a highly orchestrated process that involves over two hundred protein factors. After early assembly events on nascent rRNA in the nucleolus, pre-60S particles undergo ...Eukaryotic ribosome assembly is a highly orchestrated process that involves over two hundred protein factors. After early assembly events on nascent rRNA in the nucleolus, pre-60S particles undergo continuous maturation steps in the nucleoplasm, and prepare for nuclear export. Here, we report eleven cryo-EM structures of the nuclear pre-60S particles isolated from human cells through epitope-tagged GNL2, at resolutions of 2.8-4.3 Å. These high-resolution snapshots provide fine details for several major structural remodeling events at a virtual temporal resolution. Two new human nuclear factors, L10K and C11orf98, were also identified. Comparative structural analyses reveal that many assembly factors act as successive place holders to control the timing of factor association/dissociation events. They display multi-phasic binding properties for different domains and generate complex binding inter-dependencies as a means to guide the rRNA maturation process towards its mature conformation. Overall, our data reveal that nuclear assembly of human pre-60S particles is generally hierarchical with short branch pathways, and a few factors display specific roles as rRNA chaperones by confining rRNA helices locally to facilitate their folding, such as the C-terminal domain of SDAD1. | |||||||||||||||||||||||||||||||||
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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 | 8ir1.cif.gz | 3.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8ir1.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 8ir1.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8ir1_validation.pdf.gz | 1.9 MB | Display | wwPDB validaton report |
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| Full document | 8ir1_full_validation.pdf.gz | 2.1 MB | Display | |
| Data in XML | 8ir1_validation.xml.gz | 289.8 KB | Display | |
| Data in CIF | 8ir1_validation.cif.gz | 474.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ir/8ir1 ftp://data.pdbj.org/pub/pdb/validation_reports/ir/8ir1 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 35672MC ![]() 8idtC ![]() 8idyC ![]() 8ie3C ![]() 8ineC ![]() 8infC ![]() 8inkC ![]() 8ipdC ![]() 8ipxC ![]() 8ipyC ![]() 8ir3C 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
+60S ribosomal protein ... , 37 types, 37 molecules yBDEFGHIKLMPQSUVXZabcehilmnopA...
-Protein , 11 types, 11 molecules 467zNuvwrT9
| #2: Protein | Mass: 74107.820 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BZE4 |
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| #3: Protein | Mass: 26620.010 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P56537 |
| #4: Protein | Mass: 19666.258 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UHA3 |
| #33: Protein | Mass: 15268.361 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BRT6 |
| #37: Protein | Mass: 53387.141 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9NVX2 |
| #39: Protein | Mass: 62098.242 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9BVP2 |
| #40: Protein | Mass: 27602.535 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9UKD2 |
| #41: Protein | Mass: 83796.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q13823 |
| #42: Protein | Mass: 40312.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9H6F5 |
| #52: Protein | Mass: 35658.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q9H7B2 |
| #53: Protein | Mass: 96726.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: Q8IY81, Transferases; Transferring one-carbon groups; Methyltransferases |
-Ribosome biogenesis ... , 2 types, 2 molecules JR
| #36: Protein | Mass: 30136.703 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O95478 |
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| #38: Protein | Mass: 41278.523 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15050 |
-RNA chain , 3 types, 3 molecules 28W
| #43: RNA chain | Mass: 1636356.500 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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| #44: RNA chain | Mass: 50157.676 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: KY962518 |
| #51: RNA chain | Mass: 38691.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: GenBank: NR_023363 |
-Non-polymers , 2 types, 2 molecules 


| #54: Chemical | ChemComp-GTP / |
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| #55: Chemical | ChemComp-MG / |
-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-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 human nuclear pre-60S ribosomal particle - State A Type: RIBOSOME / Entity ID: #1-#45, #53, #46-#52 / Source: NATURAL |
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| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 |
| 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: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: OTHER |
| Electron lens | Mode: DIFFRACTION / Nominal defocus max: 1800 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 1.8 e/Å2 / Film or detector model: GATAN K2 QUANTUM (4k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.19.2_4158: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 30311 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
China, 1items
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FIELD EMISSION GUN