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Yorodumi- PDB-9kd7: The structure of RNA polymerase II elongation complex paused at N... -
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Basic information
| Entry | Database: PDB / ID: 9kd7 | |||||||||||||||||||||||||||
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| Title | The structure of RNA polymerase II elongation complex paused at N-1 state by actinomycin D. | |||||||||||||||||||||||||||
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Keywords | TRANSCRIPTION / RNA polymerase II elongation complex / actinomycin D / N-2 state structure | |||||||||||||||||||||||||||
| Function / homology | Function and homology informationRPB4-RPB7 complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / TP53 Regulates Transcription of DNA Repair Genes ...RPB4-RPB7 complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / TP53 Regulates Transcription of DNA Repair Genes / 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 / termination of RNA polymerase II transcription / RNA Polymerase II Pre-transcription Events / termination of RNA polymerase III transcription / RNA-templated transcription / Formation of TC-NER Pre-Incision Complex / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / RNA Polymerase I Promoter Escape / transcription initiation at RNA polymerase III promoter / termination of RNA polymerase I transcription / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription initiation at RNA polymerase I promoter / nucleolar large rRNA transcription by RNA polymerase I / Estrogen-dependent gene expression / transcription by RNA polymerase III / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / Dual incision in TC-NER / positive regulation of translational initiation / nuclear-transcribed mRNA catabolic process / RNA polymerase I complex / RNA polymerase III complex / transcription elongation by RNA polymerase I / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription by RNA polymerase I / translesion synthesis / transcription-coupled nucleotide-excision repair / translation initiation factor binding / transcription initiation at RNA polymerase II promoter / DNA-templated transcription initiation / transcription elongation by RNA polymerase II / P-body / mRNA transcription by RNA polymerase II / ribonucleoside binding / mRNA processing / DNA-directed RNA polymerase / cytoplasmic stress granule / DNA-directed RNA polymerase activity / peroxisome / single-stranded DNA binding / ribosome biogenesis / transcription by RNA polymerase II / nucleic acid binding / protein dimerization activity / single-stranded RNA binding / nucleotide binding / mRNA binding / nucleolus / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / metal ion binding / nucleus / cytoplasm Similarity search - Function | |||||||||||||||||||||||||||
| Biological species | ![]() Streptomyces sp. (bacteria)synthetic construct (others) | |||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.09 Å | |||||||||||||||||||||||||||
Authors | Xu, J. / Zhao, W. / Zhu, L. | |||||||||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: Nat Commun / Year: 2026Title: Stepwise transcription stalling by the anti-cancer drug Actinomycin D and insights into short tandem repeat transcription inhibition. Authors: Weiqi Zhao / Liulian Zhu / Yankai Liu / Wenjing Deng / Xu Yang / Lei Ye / Zhiyuan Lin / Kefeng Ding / Xin Yang / Xuekun Li / Jun Xu / ![]() Abstract: Short tandem repeats (STRs) comprise 6% of the human genome, and their transcription is linked to over 60 diseases. Actinomycin D (ACTD) is the first clinically approved anticancer antibiotic that ...Short tandem repeats (STRs) comprise 6% of the human genome, and their transcription is linked to over 60 diseases. Actinomycin D (ACTD) is the first clinically approved anticancer antibiotic that inhibits transcription through an incompletely understood mechanism. Here, using reconstituted yeast and mammalian systems, we investigate the mechanism of transcription inhibition and examine the impact of ACTD on STR transcription. We show that ACTD induces RNA polymerase II (Pol II) pausing at three distinct states and present structural snapshots of Pol II processing ACTD in these states. Furthermore, we examine ACTD's effects on Pol II transcribing five disease-linked, GC-rich STRs and resolve structures of Pol II in complex with ACTD during the transcription of CTG repeats associated with myotonic dystrophy type 1. Our findings reveal the structural basis of ACTD-mediated transcription inhibition and provide a framework for the rational modification of ACTD to target STR-associated disorders. | |||||||||||||||||||||||||||
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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 | 9kd7.cif.gz | 847.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9kd7.ent.gz | 667.6 KB | Display | PDB format |
| PDBx/mmJSON format | 9kd7.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kd/9kd7 ftp://data.pdbj.org/pub/pdb/validation_reports/kd/9kd7 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 62264MC ![]() 9k7fC ![]() 9kd8C ![]() 9kd9C ![]() 9kdnC ![]() 9kdoC ![]() 9kdqC 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 II subunit ... , 7 types, 7 molecules ABCDGIK
| #1: Protein | Mass: 191821.578 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: Protein | Mass: 138937.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #3: Protein | Mass: 35330.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 25451.191 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
| #7: Protein | Mass: 19081.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #9: Protein | Mass: 14308.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #11: Protein | Mass: 13633.493 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
| #5: Protein | Mass: 25117.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #6: Protein | Mass: 17931.834 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #8: Protein | Mass: 16525.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 8290.732 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #12: Protein | Mass: 7729.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-DNA chain , 2 types, 2 molecules NT
| #14: DNA chain | Mass: 15001.663 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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| #16: DNA chain | Mass: 15082.698 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Protein/peptide / RNA chain , 2 types, 2 molecules MP
| #13: Protein/peptide | |
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| #15: RNA chain | Mass: 4100.517 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Non-polymers , 2 types, 9 molecules 


| #17: Chemical | ChemComp-ZN / #18: Chemical | ChemComp-MG / | |
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-Details
| Compound details | ACTINOMYCIN D IS A BICYCLIC PEPTIDE, A MEMBER OF THE ACTINOMYCIN FAMILY. HERE, ACTINOMYCIN D IS ...ACTINOMYCI |
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| Has ligand of interest | Y |
| 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: DNA-directed RNA polymerase II elongation complex in complex with actinomycin D at n-1 state Type: COMPLEX / Entity ID: #1-#16 / Source: NATURAL |
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| Molecular weight | Value: 0.45 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 49.4 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
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| CTF correction | Type: NONE | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.09 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 60673 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 3.09 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Streptomyces sp. (bacteria)
China, 1items
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FIELD EMISSION GUN