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Yorodumi- PDB-7vba: Structure of the pre state human RNA Polymerase I Elongation Complex -
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Basic information
| Entry | Database: PDB / ID: 7vba | ||||||
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| Title | Structure of the pre state human RNA Polymerase I Elongation Complex | ||||||
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Keywords | TRANSCRIPTION/DNA/RNA / RNA Polymerase I / transcription / pre / state / TRANSCRIPTION-DNA-RNA complex | ||||||
| Function / homology | Function and homology informationRNA polymerase I transcription regulator complex / negative regulation of protein localization to nucleolus / nucleologenesis / neural crest formation / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / DNA/RNA hybrid binding / RNA polymerase I general transcription initiation factor binding / regulation of transcription by RNA polymerase I / RPAP3/R2TP/prefoldin-like complex ...RNA polymerase I transcription regulator complex / negative regulation of protein localization to nucleolus / nucleologenesis / neural crest formation / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / DNA/RNA hybrid binding / RNA polymerase I general transcription initiation factor binding / regulation of transcription by RNA polymerase I / RPAP3/R2TP/prefoldin-like 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 I preinitiation complex assembly / RNA Polymerase III Abortive And Retractive Initiation / Cytosolic sensors of pathogen-associated DNA / 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 / termination of RNA polymerase I transcription / mRNA Splicing - Minor Pathway / PIWI-interacting RNA (piRNA) biogenesis / transcription initiation at RNA polymerase I promoter / nucleolar large rRNA transcription by RNA polymerase I / Processing of Capped Intron-Containing Pre-mRNA / rRNA transcription / 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 / 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 / embryo implantation / mRNA Splicing - Major Pathway / Inhibition of DNA recombination at telomere / cell surface receptor protein tyrosine kinase signaling pathway / cellular response to leukemia inhibitory factor / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase I Promoter Escape / DNA-templated transcription initiation / 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 / chromosome / Estrogen-dependent gene expression / nucleic acid binding / transcription by RNA polymerase II / protein dimerization activity / protein stabilization / chromatin binding / chromatin / nucleolus / magnesium ion binding / mitochondrion / DNA binding / RNA binding / zinc ion binding / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.89 Å | ||||||
Authors | Zhao, D. / Liu, W. / Chen, K. / Yang, H. / Xu, Y. | ||||||
| Funding support | 1items
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Citation | Journal: Cell Discov / Year: 2021Title: Structure of the human RNA polymerase I elongation complex. Authors: Dan Zhao / Weida Liu / Ke Chen / Zihan Wu / Huirong Yang / Yanhui Xu / ![]() Abstract: Eukaryotic RNA polymerase I (Pol I) transcribes ribosomal DNA and generates RNA for ribosome synthesis. Pol I accounts for the majority of cellular transcription activity and dysregulation of Pol I ...Eukaryotic RNA polymerase I (Pol I) transcribes ribosomal DNA and generates RNA for ribosome synthesis. Pol I accounts for the majority of cellular transcription activity and dysregulation of Pol I transcription leads to cancers and ribosomopathies. Despite extensive structural studies of yeast Pol I, structure of human Pol I remains unsolved. Here we determined the structures of the human Pol I in the pre-translocation, post-translocation, and backtracked states at near-atomic resolution. The single-subunit peripheral stalk lacks contacts with the DNA-binding clamp and is more flexible than the two-subunit stalk in yeast Pol I. Compared to yeast Pol I, human Pol I possesses a more closed clamp, which makes more contacts with DNA. The Pol I structure in the post-cleavage backtracked state shows that the C-terminal zinc ribbon of RPA12 inserts into an open funnel and facilitates "dinucleotide cleavage" on mismatched DNA-RNA hybrid. Critical disease-associated mutations are mapped on Pol I regions that are involved in catalysis and complex organization. In summary, the structures provide new sights into human Pol I complex organization and efficient proofreading. | ||||||
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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 | 7vba.cif.gz | 770.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7vba.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 7vba.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7vba_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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| Full document | 7vba_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | 7vba_validation.xml.gz | 122.9 KB | Display | |
| Data in CIF | 7vba_validation.cif.gz | 187.7 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vb/7vba ftp://data.pdbj.org/pub/pdb/validation_reports/vb/7vba | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 31876MC ![]() 7vbbC ![]() 7vbcC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Assembly
| Deposited unit | ![]()
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Components
-DNA-directed RNA polymerase I subunit ... , 6 types, 6 molecules ABINGM
| #1: Protein | Mass: 194911.859 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR1A / Production host: Homo sapiens (human) / References: UniProt: O95602, DNA-directed RNA polymerase |
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| #2: Protein | Mass: 128379.219 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR1B / Production host: Homo sapiens (human) / References: UniProt: Q9H9Y6, DNA-directed RNA polymerase |
| #7: Protein | Mass: 13917.695 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR1H, RPA12, ZNRD1 / Production host: Homo sapiens (human) / References: UniProt: Q9P1U0 |
| #11: Protein | Mass: 55065.523 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR1G, ASE1, CAST, CD3EAP, PAF49 / Production host: Homo sapiens (human) / References: UniProt: O15446 |
| #12: Protein | Mass: 37490.379 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR1F, TWISTNB / Production host: Homo sapiens (human) / References: UniProt: Q3B726 |
| #13: Protein | Mass: 47330.234 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR1E, PAF53, PRAF1 / Production host: Homo sapiens (human) / References: UniProt: Q9GZS1 |
-DNA-directed RNA polymerases I and III subunit ... , 2 types, 2 molecules CK
| #3: Protein | Mass: 39301.672 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR1C, POLR1E / Production host: Homo sapiens (human) / References: UniProt: O15160 |
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| #9: Protein | Mass: 15259.222 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR1D / Production host: Homo sapiens (human) / References: UniProt: P0DPB6 |
-DNA-directed RNA polymerases I, II, and III subunit ... , 5 types, 5 molecules EFHJL
| #4: Protein | Mass: 24584.223 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR2E / Production host: Homo sapiens (human) / References: UniProt: P19388 |
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| #5: Protein | Mass: 14491.026 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR2F, POLRF / Production host: Homo sapiens (human) / References: UniProt: P61218 |
| #6: Protein | Mass: 17162.273 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR2H / Production host: Homo sapiens (human) / References: UniProt: P52434 |
| #8: Protein | Mass: 7655.123 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR2L / Production host: Homo sapiens (human) / References: UniProt: P62875 |
| #10: Protein | Mass: 7018.244 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR2K / Production host: Homo sapiens (human) / References: UniProt: P53803 |
-RNA chain , 1 types, 1 molecules R
| #14: RNA chain | Mass: 2503.521 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
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-DNA chain , 2 types, 2 molecules TU
| #15: DNA chain | Mass: 6804.421 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
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| #16: DNA chain | Mass: 3918.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
-Non-polymers , 3 types, 7 molecules 




| #17: Chemical | ChemComp-ZN / #18: Chemical | ChemComp-MG / | #19: Chemical | ChemComp-2TM / | |
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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 RNA Polymerase I Elongation Complex / Type: COMPLEX / Entity ID: #1-#16 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.4 |
| 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: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.16_3549: / Classification: refinement | ||||||||||||||||||||||||
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| CTF correction | Type: NONE | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.89 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 382890 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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