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Open data
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Basic information
| Entry | Database: PDB / ID: 8qw9 | ||||||||||||||||||||||||
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| Title | RNAPII elongation complex bound to RECQ5_R502E | ||||||||||||||||||||||||
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Keywords | TRANSCRIPTION / RNA polymerase II / transcription inhibition / electron cryomicroscopy / electron cryotomography | ||||||||||||||||||||||||
| Function / homology | Function and homology informationFormation of RNA Pol II elongation complex / Formation of the Early Elongation Complex / Transcriptional regulation by small RNAs / FGFR2 alternative splicing / RNA polymerase II transcribes snRNA genes / mRNA Capping / mRNA Splicing - Minor Pathway / RNA Polymerase I Transcription Initiation / RNA Polymerase I Promoter Escape / RNA Polymerase II Promoter Escape ...Formation of RNA Pol II elongation complex / Formation of the Early Elongation Complex / Transcriptional regulation by small RNAs / FGFR2 alternative splicing / RNA polymerase II transcribes snRNA genes / mRNA Capping / mRNA Splicing - Minor Pathway / RNA Polymerase I Transcription Initiation / RNA Polymerase I Promoter Escape / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase I Transcription Termination / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / 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 Pol II CTD phosphorylation and interaction with CE / Estrogen-dependent gene expression / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Transcription Elongation / Processing of Capped Intron-Containing Pre-mRNA / B-WICH complex positively regulates rRNA expression / mitotic DNA-templated DNA replication / mRNA Splicing - Major Pathway / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / chromosome separation / cellular response to camptothecin / DNA/RNA hybrid binding / four-way junction helicase activity / replication-born double-strand break repair via sister chromatid exchange / transcription preinitiation complex / DNA 3'-5' helicase / DNA metabolic process / 3'-5' DNA helicase activity / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / RNA polymerase II complex binding / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / nuclear-transcribed mRNA catabolic process / positive regulation of translational initiation / negative regulation of transcription elongation by RNA polymerase II / negative regulation of double-strand break repair via homologous recombination / RNA polymerase I complex / transcription elongation by RNA polymerase I / RNA polymerase III complex / core promoter sequence-specific DNA binding / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription by RNA polymerase I / translation initiation factor binding / transcription-coupled nucleotide-excision repair / DNA helicase activity / replication fork / transcription initiation at RNA polymerase II promoter / P-body / euchromatin / helicase activity / protein-DNA complex / double-strand break repair via homologous recombination / ribonucleoside binding / cellular response to xenobiotic stimulus / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / mitotic cell cycle / single-stranded DNA binding / chromosome / Hydrolases; Acting on ester bonds; Exoribonucleases producing 5'-phosphomonoesters / nucleic acid binding / transcription by RNA polymerase II / chromosome, telomeric region / DNA replication / single-stranded RNA binding / protein dimerization activity / hydrolase activity / RNA-directed RNA polymerase / cell division / DNA repair / nucleotide binding / RNA-directed RNA polymerase activity / chromatin binding / nucleolus / magnesium ion binding / ATP hydrolysis activity / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / ATP binding / metal ion binding / identical protein binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Homo sapiens (human)![]() synthetic construct (others) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.3 Å | ||||||||||||||||||||||||
Authors | Skubnik, K. / Sebesta, M. / Stefl, R. | ||||||||||||||||||||||||
| Funding support | Czech Republic, 1items
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Citation | Journal: To Be PublishedTitle: Spatial organization of RNA polymerase II-RECQ5 transcriptional condensate Authors: Sebesta, M. / Skubnik, K. / Stefl, R. | ||||||||||||||||||||||||
| 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 | 8qw9.cif.gz | 757.4 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8qw9.ent.gz | 590.6 KB | Display | PDB format |
| PDBx/mmJSON format | 8qw9.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8qw9_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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| Full document | 8qw9_full_validation.pdf.gz | 1.8 MB | Display | |
| Data in XML | 8qw9_validation.xml.gz | 116.7 KB | Display | |
| Data in CIF | 8qw9_validation.cif.gz | 180.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qw/8qw9 ftp://data.pdbj.org/pub/pdb/validation_reports/qw/8qw9 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 18683MC ![]() 8qq2C ![]() 8qw8C 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
-DNA-directed RNA polymerase ... , 6 types, 6 molecules ABCIKG
| #1: Protein | Mass: 217436.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: Protein | Mass: 134041.422 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #3: Protein | Mass: 31466.098 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #7: Protein | Mass: 14507.205 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 13310.284 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein | Mass: 19314.283 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-DNA-directed RNA polymerases I, II, and III subunit ... , 5 types, 5 molecules EFHJL
| #4: Protein | Mass: 24514.219 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #5: Protein | Mass: 14491.026 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #6: Protein | Mass: 17162.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 7655.123 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 7018.244 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 2 types, 2 molecules DR
| #11: Protein | Mass: 16347.255 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #16: Protein | Mass: 72471.594 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RECQL5 / Production host: ![]() |
-RNA chain , 1 types, 1 molecules P
| #13: RNA chain | Mass: 5320.109 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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-DNA, DNA-RNA ELONGATION ... , 2 types, 2 molecules TN
| #14: DNA chain | Mass: 15780.168 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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| #15: DNA chain | Mass: 16861.730 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Non-polymers , 2 types, 8 molecules 


| #17: Chemical | ChemComp-ZN / #18: Chemical | ChemComp-MG / | |
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-Details
| Has ligand of interest | Y |
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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
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| Molecular weight | Value: 0.5 MDa / Experimental value: NO | ||||||||||||||||||||||||||||||
| Source (natural) |
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| Source (recombinant) |
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| Buffer solution | pH: 7.5 | ||||||||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
| Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 | ||||||||||||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE-PROPANE / Humidity: 100 % / Chamber temperature: 278 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: 2400 nm / Nominal defocus min: 1200 nm / Cs: 2.7 mm / C2 aperture diameter: 30 µm / Alignment procedure: COMA FREE |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 9046 |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||
| Particle selection | Num. of particles selected: 787289 | |||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | |||||||||||||||||||||
| 3D reconstruction | Resolution: 4.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 19142 / Num. of class averages: 1 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)

Czech Republic, 1items
Citation








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FIELD EMISSION GUN