+Open data
-Basic information
Entry | Database: PDB / ID: 7dn3 | ||||||
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Title | Structure of Human RNA Polymerase III elongation complex | ||||||
Components |
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Keywords | TRANSCRIPTION / RNA Polymerase III | ||||||
Function / homology | Function and homology information snRNA transcription by RNA polymerase III / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / calcitonin gene-related peptide receptor activity / DNA/RNA hybrid binding / regulation of transcription by RNA polymerase I / regulation of transcription by RNA polymerase III / RPAP3/R2TP/prefoldin-like complex / DNA polymerase III complex / Cytosolic sensors of pathogen-associated DNA ...snRNA transcription by RNA polymerase III / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / calcitonin gene-related peptide receptor activity / DNA/RNA hybrid binding / regulation of transcription by RNA polymerase I / regulation of transcription by RNA polymerase III / RPAP3/R2TP/prefoldin-like complex / DNA polymerase III complex / Cytosolic sensors of pathogen-associated DNA / 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 / positive regulation of innate immune response / Abortive elongation of HIV-1 transcript in the absence of Tat / nucleobase-containing compound metabolic process / RNA Polymerase I Transcription Termination / FGFR2 alternative splicing / 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 / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / mRNA Capping / PIWI-interacting RNA (piRNA) biogenesis / 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 / termination of RNA polymerase III transcription / transcription initiation at RNA polymerase III promoter / RNA polymerase III activity / mRNA Splicing - Minor Pathway / RNA Polymerase I Transcription Initiation / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / transcription by RNA polymerase I / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Processing of Capped Intron-Containing Pre-mRNA / transcription by RNA polymerase III / RNA polymerase II transcribes snRNA genes / neuropeptide signaling pathway / Tat-mediated elongation of the HIV-1 transcript / transcription elongation by RNA polymerase I / Formation of HIV-1 elongation complex containing HIV-1 Tat / tRNA transcription by RNA polymerase III / RNA polymerase I complex / RNA polymerase I activity / RNA polymerase III complex / Formation of HIV elongation complex in the absence of HIV Tat / RNA polymerase II, core complex / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / Inhibition of DNA recombination at telomere / positive regulation of interferon-beta production / mRNA Splicing - Major Pathway / acrosomal vesicle / protein-DNA complex / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / 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 / fibrillar center / Activation of anterior HOX genes in hindbrain development during early embryogenesis / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / single-stranded DNA binding / 4 iron, 4 sulfur cluster binding / double-stranded DNA binding / defense response to virus / Estrogen-dependent gene expression / transcription by RNA polymerase II / cell population proliferation / nucleic acid binding / protein dimerization activity / protein stabilization / nuclear body / intracellular membrane-bounded organelle / innate immune response / nucleotide binding / centrosome / DNA-templated transcription / chromatin binding / magnesium ion binding / DNA binding / zinc ion binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||
Authors | Li, L. / Yu, Z. / Zhao, D. / Ren, Y. / Hou, H. / Xu, Y. | ||||||
Citation | Journal: Cell Res / Year: 2021 Title: Structure of human RNA polymerase III elongation complex. Authors: Liang Li / Zishuo Yu / Dan Zhao / Yulei Ren / Haifeng Hou / Yanhui Xu / Abstract: RNA polymerase III (Pol III) transcribes essential structured small RNAs, such as tRNAs, 5S rRNA and U6 snRNA. The transcriptional activity of Pol III is tightly controlled and its dysregulation is ...RNA polymerase III (Pol III) transcribes essential structured small RNAs, such as tRNAs, 5S rRNA and U6 snRNA. The transcriptional activity of Pol III is tightly controlled and its dysregulation is associated with human diseases, such as cancer. Human Pol III has two isoforms with difference only in one of its subunits RPC7 (α and β). Despite structural studies of yeast Pol III, structure of human Pol III remains unsolved. Here, we determined the structures of 17-subunit human Pol IIIα complex in the backtracked and post-translocation states, respectively. Human Pol III contains a generally conserved catalytic core, similar to that of yeast counterpart, and structurally unique RPC3-RPC6-RPC7 heterotrimer and RPC10. The N-ribbon of TFIIS-like RPC10 docks on the RPC4-RPC5 heterodimer and the C-ribbon inserts into the funnel of Pol III in the backtracked state but is more flexible in the post-translocation state. RPC7 threads through the heterotrimer and bridges the stalk and Pol III core module. The winged helix 1 domain of RPC6 and the N-terminal region of RPC7α stabilize each other and may prevent Maf1-mediated repression of Pol III activity. The C-terminal FeS cluster of RPC6 coordinates a network of interactions that mediate core-heterotrimer contacts and stabilize Pol III. Our structural analysis sheds new light on the molecular mechanism of human Pol IIIα-specific transcriptional regulation and provides explanations for upregulated Pol III activity in RPC7α-dominant cancer cells. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7dn3.cif.gz | 864.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7dn3.ent.gz | 673.9 KB | Display | PDB format |
PDBx/mmJSON format | 7dn3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7dn3_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 7dn3_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | 7dn3_validation.xml.gz | 131.2 KB | Display | |
Data in CIF | 7dn3_validation.cif.gz | 201.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dn/7dn3 ftp://data.pdbj.org/pub/pdb/validation_reports/dn/7dn3 | HTTPS FTP |
-Related structure data
Related structure data | 30779MC 7du2C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-DNA-directed RNA polymerase III subunit ... , 10 types, 10 molecules ABGIPOQDMN
#1: Protein | Mass: 155860.125 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR3A / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: O14802, DNA-directed RNA polymerase |
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#2: Protein | Mass: 127953.891 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR3B / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q9NW08, DNA-directed RNA polymerase |
#4: Protein | Mass: 22938.846 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR3H, KIAA1665, RPC8 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q9Y535 |
#5: Protein | Mass: 12354.104 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR3K, RPC11, My010 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q9Y2Y1 |
#8: Protein | Mass: 35726.914 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR3F / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q9H1D9 |
#13: Protein | Mass: 60692.555 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR3C / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q9BUI4 |
#14: Protein | Mass: 25953.510 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR3G / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: O15318 |
#15: Protein | Mass: 16893.990 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CRCP / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: O75575 |
#16: Protein | Mass: 80004.031 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR3E, KIAA1452 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q9NVU0 |
#17: Protein | Mass: 44471.875 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: POLR3D, BN51, BN51T / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P05423 |
-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 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: O15160 |
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#6: 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 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P0DPB6 |
-DNA-directed RNA polymerases I, II, and III subunit ... , 5 types, 5 molecules LEFHJ
#7: 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 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P53803 |
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#9: 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 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P19388 |
#10: 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 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P61218 |
#11: 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 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P52434 |
#12: 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 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P62875 |
-DNA chain , 2 types, 2 molecules XY
#18: DNA chain | Mass: 4889.178 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293 / Production host: Homo sapiens (human) |
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#19: DNA chain | Mass: 7130.611 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293 / Production host: Homo sapiens (human) |
-RNA chain , 1 types, 1 molecules R
#20: RNA chain | Mass: 1851.165 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293 / Production host: Homo sapiens (human) |
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-Non-polymers , 3 types, 8 molecules
#21: Chemical | ChemComp-MG / | ||
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#22: Chemical | ChemComp-ZN / #23: Chemical | ChemComp-SF4 / | |
-Details
Has ligand of interest | 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 |
-Sample preparation
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Source (natural) |
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Source (recombinant) |
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Buffer solution | pH: 8 | ||||||||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
-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 K3 (6k x 4k) |
-Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 98293 / Symmetry type: POINT |