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Open data
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Basic information
| Entry | Database: PDB / ID: 5ivw | |||||||||||||||
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| Title | Human core TFIIH bound to DNA within the PIC | |||||||||||||||
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Keywords | TRANSCRIPTION/DNA / initiation / RNA polymerase II / human / TRANSCRIPTION-DNA complex | |||||||||||||||
| Function / homology | Function and homology informationMMXD complex / core TFIIH complex portion of holo TFIIH complex / Cytosolic iron-sulfur cluster assembly / central nervous system myelin formation / positive regulation of mitotic recombination / hair cell differentiation / hair follicle maturation / nucleotide-excision repair factor 3 complex / nucleotide-excision repair, preincision complex assembly / CAK-ERCC2 complex ...MMXD complex / core TFIIH complex portion of holo TFIIH complex / Cytosolic iron-sulfur cluster assembly / central nervous system myelin formation / positive regulation of mitotic recombination / hair cell differentiation / hair follicle maturation / nucleotide-excision repair factor 3 complex / nucleotide-excision repair, preincision complex assembly / CAK-ERCC2 complex / embryonic cleavage / DNA 5'-3' helicase / UV protection / G protein-coupled receptor internalization / transcription factor TFIIH core complex / transcription factor TFIIH holo complex / transcription preinitiation complex / RNA Polymerase I Transcription Termination / regulation of mitotic cell cycle phase transition / DNA 3'-5' helicase / RNA polymerase II general transcription initiation factor activity / transcription factor TFIID complex / erythrocyte maturation / 3'-5' DNA helicase activity / hematopoietic stem cell proliferation / spinal cord development / 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 / bone mineralization / mRNA Capping / intrinsic apoptotic signaling pathway by p53 class mediator / ATPase activator activity / DNA topological change / RNA Polymerase I Transcription Initiation / hematopoietic stem cell differentiation / embryonic organ development / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / transcription elongation by RNA polymerase I / response to UV / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / transcription-coupled nucleotide-excision repair / extracellular matrix organization / RNA Polymerase II Pre-transcription Events / DNA helicase activity / insulin-like growth factor receptor signaling pathway / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / determination of adult lifespan / post-embryonic development / nucleotide-excision repair / chromosome segregation / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / promoter-specific chromatin binding / RNA Polymerase I Promoter Escape / cellular response to gamma radiation / NoRC negatively regulates rRNA expression / Dual Incision in GG-NER / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / spindle / multicellular organism growth / Formation of Incision Complex in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / intracellular protein localization / 4 iron, 4 sulfur cluster binding / response to oxidative stress / double-stranded DNA binding / 5'-3' DNA helicase activity / protein-macromolecule adaptor activity / in utero embryonic development / damaged DNA binding / transcription by RNA polymerase II / response to hypoxia / nuclear speck / positive regulation of apoptotic process / DNA repair / apoptotic process / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / nucleolus / ATP hydrolysis activity / DNA binding / zinc ion binding / nucleoplasm / ATP binding / metal ion binding Similarity search - Function | |||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 10 Å | |||||||||||||||
Authors | He, Y. / Yan, C. / Fang, J. / Inouye, C. / Tjian, R. / Ivanov, I. / Nogales, E. | |||||||||||||||
| Funding support | United States, 4items
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Citation | Journal: Nature / Year: 2016Title: Near-atomic resolution visualization of human transcription promoter opening. Authors: Yuan He / Chunli Yan / Jie Fang / Carla Inouye / Robert Tjian / Ivaylo Ivanov / Eva Nogales / ![]() Abstract: In eukaryotic transcription initiation, a large multi-subunit pre-initiation complex (PIC) that assembles at the core promoter is required for the opening of the duplex DNA and identification of the ...In eukaryotic transcription initiation, a large multi-subunit pre-initiation complex (PIC) that assembles at the core promoter is required for the opening of the duplex DNA and identification of the start site for transcription by RNA polymerase II. Here we use cryo-electron microscropy (cryo-EM) to determine near-atomic resolution structures of the human PIC in a closed state (engaged with duplex DNA), an open state (engaged with a transcription bubble), and an initially transcribing complex (containing six base pairs of DNA-RNA hybrid). Our studies provide structures for previously uncharacterized components of the PIC, such as TFIIE and TFIIH, and segments of TFIIA, TFIIB and TFIIF. Comparison of the different structures reveals the sequential conformational changes that accompany the transition from each state to the next throughout the transcription initiation process. This analysis illustrates the key role of TFIIB in transcription bubble stabilization and provides strong structural support for a translocase activity of XPB. | |||||||||||||||
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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 | 5ivw.cif.gz | 382.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb5ivw.ent.gz | 276.6 KB | Display | PDB format |
| PDBx/mmJSON format | 5ivw.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 5ivw_validation.pdf.gz | 765.6 KB | Display | wwPDB validaton report |
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| Full document | 5ivw_full_validation.pdf.gz | 963.7 KB | Display | |
| Data in XML | 5ivw_validation.xml.gz | 80.5 KB | Display | |
| Data in CIF | 5ivw_validation.cif.gz | 114.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iv/5ivw ftp://data.pdbj.org/pub/pdb/validation_reports/iv/5ivw | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8131MC ![]() 8132C ![]() 8133C ![]() 8134C ![]() 8135C ![]() 8136C ![]() 8137C ![]() 8138C ![]() 5iy6C ![]() 5iy7C ![]() 5iy8C ![]() 5iy9C ![]() 5iyaC ![]() 5iybC ![]() 5iycC ![]() 5iydC 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
-TFIIH basal transcription factor complex helicase ... , 2 types, 2 molecules VW
| #1: Protein | Mass: 89404.734 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P19447, DNA helicase |
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| #2: Protein | Mass: 87021.078 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P18074, DNA helicase |
-General transcription factor IIH subunit ... , 4 types, 4 molecules 0123
| #3: Protein | Mass: 44481.996 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q13888 |
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| #4: Protein | Mass: 8060.362 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q6ZYL4 |
| #5: Protein | Mass: 52245.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q92759 |
| #6: Protein | Mass: 34416.008 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q13889 |
-DNA chain , 2 types, 2 molecules XY
| #7: DNA chain | Mass: 5879.866 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
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| #8: DNA chain | Mass: 6071.922 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
-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 core TFIIH bound to DNA within the PIC / Type: COMPLEX / Entity ID: all / Source: NATURAL |
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| Molecular weight | Value: 0.49 MDa / Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.9 |
| Specimen | Conc.: 0.1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % Details: Blot for 4 seconds before plunging into liquid ethane (FEI VITROBOT MARK IV). |
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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 magnification: 27500 X / Nominal defocus max: 4000 nm / Nominal defocus min: 2000 nm / Cs: 2.7 mm |
| Specimen holder | Specimen holder model: GATAN 626 SINGLE TILT LIQUID NITROGEN CRYO TRANSFER HOLDER |
| Image recording | Electron dose: 42 e/Å2 / Detector mode: COUNTING / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
| Image scans | Movie frames/image: 30 |
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Processing
| EM software | Name: RELION / Version: 1.4beta / Category: 3D reconstruction |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3D reconstruction | Resolution: 10 Å / Resolution method: FSC 0.5 CUT-OFF / Num. of particles: 219771 / Symmetry type: POINT |
| Atomic model building | Protocol: FLEXIBLE FIT |
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About Yorodumi




Homo sapiens (human)
United States, 4items
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