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Open data
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Basic information
| Entry | Database: PDB / ID: 7ast | ||||||||||||
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| Title | Apo Human RNA Polymerase III | ||||||||||||
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Keywords | TRANSCRIPTION / RNA Polymerase III / tRNA | ||||||||||||
| Function / homology | Function and homology informationsnRNA transcription by RNA polymerase III / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / DNA/RNA hybrid binding / calcitonin gene-related peptide receptor activity / regulation of transcription by RNA polymerase III / regulation of transcription by RNA polymerase I / RPAP3/R2TP/prefoldin-like complex / DNA polymerase III complex / RNA Polymerase III Transcription Initiation From Type 1 Promoter ...snRNA transcription by RNA polymerase III / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / DNA/RNA hybrid binding / calcitonin gene-related peptide receptor activity / regulation of transcription by RNA polymerase III / regulation of transcription by RNA polymerase I / RPAP3/R2TP/prefoldin-like complex / DNA polymerase III complex / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Polymerase III Transcription Initiation From Type 3 Promoter / RNA Polymerase III Abortive And Retractive Initiation / Cytosolic sensors of pathogen-associated DNA / positive regulation of innate immune response / nucleobase-containing compound metabolic process / Abortive elongation of HIV-1 transcript in the absence of Tat / FGFR2 alternative splicing / RNA Polymerase I Transcription Termination / MicroRNA (miRNA) biogenesis / Viral Messenger RNA Synthesis / Signaling by FGFR2 IIIa TM / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / HIV Transcription Initiation / RNA Polymerase II HIV Promoter Escape / Transcription of the HIV genome / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / mRNA Capping / transcription initiation at RNA polymerase III promoter / mRNA Splicing - Minor Pathway / PIWI-interacting RNA (piRNA) biogenesis / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase I Transcription Initiation / transcription by RNA polymerase III / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / RNA polymerase II transcribes snRNA genes / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / neuropeptide signaling pathway / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / RNA polymerase I complex / transcription elongation by RNA polymerase I / RNA polymerase III complex / Formation of HIV elongation complex in the absence of HIV Tat / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription by RNA polymerase I / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / acrosomal vesicle / mRNA Splicing - Major Pathway / Inhibition of DNA recombination at telomere / positive regulation of interferon-beta production / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / protein-DNA complex / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / ribonucleoside binding / Activation of anterior HOX genes in hindbrain development during early embryogenesis / fibrillar center / DNA-directed RNA polymerase / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / DNA-directed RNA polymerase activity / single-stranded DNA binding / 4 iron, 4 sulfur cluster binding / double-stranded DNA binding / defense response to virus / Estrogen-dependent gene expression / nucleic acid binding / transcription by RNA polymerase II / protein dimerization activity / protein stabilization / innate immune response / nucleotide binding / intracellular membrane-bounded organelle / DNA-templated transcription / centrosome / chromatin binding / magnesium ion binding / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / nucleus / membrane / plasma membrane Similarity search - Function | ||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4 Å | ||||||||||||
Authors | Ramsay, E.P. / Abascal-Palacios, G. / Daiss, J.L. / King, H. / Gouge, J. / Pilsl, M. / Beuron, F. / Morris, E. / Gunkel, P. / Engel, C. / Vannini, A. | ||||||||||||
| Funding support | United Kingdom, Germany, 3items
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Citation | Journal: Nat Commun / Year: 2020Title: Structure of human RNA polymerase III. Authors: Ewan Phillip Ramsay / Guillermo Abascal-Palacios / Julia L Daiß / Helen King / Jerome Gouge / Michael Pilsl / Fabienne Beuron / Edward Morris / Philip Gunkel / Christoph Engel / Alessandro Vannini / ![]() Abstract: In eukaryotes, RNA Polymerase (Pol) III is specialized for the transcription of tRNAs and other short, untranslated RNAs. Pol III is a determinant of cellular growth and lifespan across eukaryotes. ...In eukaryotes, RNA Polymerase (Pol) III is specialized for the transcription of tRNAs and other short, untranslated RNAs. Pol III is a determinant of cellular growth and lifespan across eukaryotes. Upregulation of Pol III transcription is observed in cancer and causative Pol III mutations have been described in neurodevelopmental disorders and hypersensitivity to viral infection. Here, we report a cryo-EM reconstruction at 4.0 Å of human Pol III, allowing mapping and rationalization of reported genetic mutations. Mutations causing neurodevelopmental defects cluster in hotspots affecting Pol III stability and/or biogenesis, whereas mutations affecting viral sensing are located in proximity to DNA binding regions, suggesting an impairment of Pol III cytosolic viral DNA-sensing. Integrating x-ray crystallography and SAXS, we also describe the structure of the higher eukaryote specific RPC5 C-terminal extension. Surprisingly, experiments in living cells highlight a role for this module in the assembly and stability of human Pol III. | ||||||||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7ast.cif.gz | 802.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7ast.ent.gz | 625.9 KB | Display | PDB format |
| PDBx/mmJSON format | 7ast.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7ast_validation.pdf.gz | 964.9 KB | Display | wwPDB validaton report |
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| Full document | 7ast_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | 7ast_validation.xml.gz | 144.7 KB | Display | |
| Data in CIF | 7ast_validation.cif.gz | 216 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/as/7ast ftp://data.pdbj.org/pub/pdb/validation_reports/as/7ast | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 11904MC ![]() 7asuC ![]() 7asvC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-DNA-directed RNA polymerase III subunit ... , 10 types, 10 molecules NAIJKLMZXY
| #1: Protein | Mass: 155860.125 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: O14802, DNA-directed RNA polymerase |
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| #2: Protein | Mass: 12354.104 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: Q9Y2Y1 |
| #10: Protein | Mass: 16893.990 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: O75575 |
| #11: Protein | Mass: 22938.846 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: Q9Y535 |
| #12: Protein | Mass: 80004.031 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: Q9NVU0 |
| #13: Protein | Mass: 44471.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: P05423 |
| #14: Protein | Mass: 127953.891 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: Q9NW08, DNA-directed RNA polymerase |
| #15: Protein | Mass: 35726.914 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: Q9H1D9 |
| #16: Protein | Mass: 60692.555 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: Q9BUI4 |
| #17: Protein/peptide | Mass: 3081.790 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa |
-DNA-directed RNA polymerases I, II, and III subunit ... , 5 types, 5 molecules BCDEF
| #3: Protein | Mass: 7655.123 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: P62875 |
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| #4: Protein | Mass: 7018.244 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: P53803 |
| #5: Protein | Mass: 17162.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: P52434 |
| #6: Protein | Mass: 14491.026 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: P61218 |
| #7: Protein | Mass: 24584.223 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: P19388 |
-DNA-directed RNA polymerases I and III subunit ... , 2 types, 2 molecules GH
| #8: Protein | Mass: 15259.222 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: P0DPB6 |
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| #9: Protein | Mass: 39301.672 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: O15160 |
-Details
| Has protein modification | Y |
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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 RNA Polymerase III / Type: COMPLEX Details: The human RNA polymerase III complex purified from HeLa cells. Entity ID: all / Source: NATURAL | ||||||||||||||||||||||||||||||
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| Molecular weight | Experimental value: NO | ||||||||||||||||||||||||||||||
| Source (natural) | Organism: Homo sapiens (human) / Cellular location: Nucleus and cytoplasm | ||||||||||||||||||||||||||||||
| Buffer solution | pH: 8 | ||||||||||||||||||||||||||||||
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| Specimen | Conc.: 0.06 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES Details: The sample was monodisperse with well-defined complex particles. | ||||||||||||||||||||||||||||||
| Specimen support | Grid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: C-flat-1.2/1.3 | ||||||||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 291 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: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 75000 X / Cs: 2.7 mm / C2 aperture diameter: 70 µm |
| Specimen holder | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Average exposure time: 70 sec. / Electron dose: 40.8 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.18.1_3865: / Classification: refinement | ||||||||||||||||||||||||||||||||||||
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| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 25369 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
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About Yorodumi




Homo sapiens (human)
United Kingdom,
Germany, 3items
Citation
UCSF Chimera












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