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Open data
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Basic information
| Entry | Database: PDB / ID: 5iyc | |||||||||||||||
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| Title | Human core-PIC in the initial transcribing state | |||||||||||||||
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Keywords | TRANSCRIPTION / TRANSFERASE/DNA / initiation / RNA polymerase II / human / TRANSFERASE-DNA complex | |||||||||||||||
| Function / homology | Function and homology informationmicrofibril binding / RNA Polymerase III Chain Elongation / positive regulation of core promoter binding / RNA polymerase II core complex assembly / RNA Polymerase III Transcription Termination / transcription factor TFIIE complex / RNA polymerase transcription factor SL1 complex / meiotic sister chromatid cohesion / phosphatase activator activity / regulation of transcription by RNA polymerase I ...microfibril binding / RNA Polymerase III Chain Elongation / positive regulation of core promoter binding / RNA polymerase II core complex assembly / RNA Polymerase III Transcription Termination / transcription factor TFIIE complex / RNA polymerase transcription factor SL1 complex / meiotic sister chromatid cohesion / phosphatase activator activity / regulation of transcription by RNA polymerase I / RNA polymerase III general transcription initiation factor activity / TFIIF-class transcription factor complex binding / transcriptional start site selection at RNA polymerase II promoter / RNA polymerase I core promoter sequence-specific DNA binding / RPAP3/R2TP/prefoldin-like complex / transcription factor TFIIF 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 / transcription factor TFIIA complex / female germ cell nucleus / RNA Polymerase III Abortive And Retractive Initiation / Cytosolic sensors of pathogen-associated DNA / male pronucleus / female pronucleus / germinal vesicle / RNA polymerase II general transcription initiation factor binding / nuclear thyroid hormone receptor binding / Abortive elongation of HIV-1 transcript in the absence of Tat / FGFR2 alternative splicing / transcription preinitiation complex / RNA Polymerase I Transcription Termination / MicroRNA (miRNA) biogenesis / Viral Messenger RNA Synthesis / Signaling by FGFR2 IIIa TM / LRR domain binding / RNA polymerase II general transcription initiation factor activity / protein acetylation / transcription factor TFIID complex / cell division site / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / acetyltransferase activity / 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 / mRNA Splicing - Minor Pathway / PIWI-interacting RNA (piRNA) biogenesis / aryl hydrocarbon receptor binding / RNA polymerase II complex binding / viral transcription / TFIIB-class transcription factor binding / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / nuclear-transcribed mRNA catabolic process / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase I Transcription Initiation / positive regulation of translational 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 / positive regulation of transcription initiation by RNA polymerase II / 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 / histone acetyltransferase activity / RNA polymerase II core promoter sequence-specific DNA binding / core promoter sequence-specific DNA binding / Formation of HIV elongation complex in the absence of HIV Tat / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / negative regulation of protein binding / RNA polymerase II preinitiation complex assembly / histone acetyltransferase / transcription by RNA polymerase I / spindle assembly / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / translation initiation factor binding / transcription-coupled nucleotide-excision repair / RNA Polymerase II Pre-transcription Events / mRNA Splicing - Major Pathway / Inhibition of DNA recombination at telomere / TBP-class protein binding / positive regulation of RNA splicing / SIRT1 negatively regulates rRNA expression / erythrocyte differentiation / male germ cell nucleus Similarity search - Function | |||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 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 | 5iyc.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb5iyc.ent.gz | 815 KB | Display | PDB format |
| PDBx/mmJSON format | 5iyc.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 5iyc_validation.pdf.gz | 958.8 KB | Display | wwPDB validaton report |
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| Full document | 5iyc_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | 5iyc_validation.xml.gz | 169.7 KB | Display | |
| Data in CIF | 5iyc_validation.cif.gz | 255.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iy/5iyc ftp://data.pdbj.org/pub/pdb/validation_reports/iy/5iyc | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8137MC ![]() 8131C ![]() 8132C ![]() 8133C ![]() 8134C ![]() 8135C ![]() 8136C ![]() 8138C ![]() 5ivwC ![]() 5iy6C ![]() 5iy7C ![]() 5iy8C ![]() 5iy9C ![]() 5iyaC ![]() 5iybC ![]() 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
-DNA-directed RNA polymerase II subunit ... , 12 types, 12 molecules ABCDEFGHIJKL
| #1: Protein | Mass: 217420.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P24928, DNA-directed RNA polymerase, RNA-directed RNA polymerase |
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| #2: Protein | Mass: 134071.453 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P30876, DNA-directed RNA polymerase |
| #3: Protein | Mass: 31478.148 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P19387 |
| #4: Protein | Mass: 16331.255 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O15514 |
| #5: Protein | Mass: 24584.223 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P19388 |
| #6: Protein | Mass: 14491.026 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P61218 |
| #7: Protein | Mass: 19314.283 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62487 |
| #8: Protein | Mass: 17162.273 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P52434 |
| #9: Protein | Mass: 14541.221 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P36954 |
| #10: Protein | Mass: 7655.123 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P62875 |
| #11: Protein | Mass: 13310.284 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P52435 |
| #12: Protein | Mass: 7018.244 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P53803 |
-Transcription initiation factor ... , 4 types, 4 molecules MNOR
| #13: Protein | Mass: 34877.949 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2B, TF2B, TFIIB / Production host: ![]() |
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| #14: Protein | Mass: 41544.551 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2A1, TF2A1 / Production host: ![]() |
| #15: Protein | Mass: 12469.091 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2A2, TF2A2 / Production host: ![]() |
| #18: Protein | Mass: 33106.824 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2E2, TF2E2 / Production host: ![]() |
-Protein , 3 types, 3 molecules PQU
| #16: Protein | Mass: 37729.938 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TBP, GTF2D1, TF2D, TFIID / Production host: ![]() |
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| #17: Protein | Mass: 49516.094 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2E1, TF2E1 / Production host: ![]() |
| #21: Protein | Mass: 34022.723 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TCEA1, GTF2S, TFIIS / Production host: ![]() |
-General transcription factor IIF subunit ... , 2 types, 2 molecules ST
| #19: Protein | Mass: 58343.578 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2F1, RAP74 / Production host: ![]() |
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| #20: Protein | Mass: 28427.309 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2F2, RAP30 / Production host: ![]() |
-DNA chain , 2 types, 2 molecules XY
| #22: DNA chain | Mass: 24800.826 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
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| #23: DNA chain | Mass: 24513.598 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
-Non-polymers , 2 types, 13 molecules 


| #24: Chemical | | #25: Chemical | ChemComp-ZN / |
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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
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| Buffer solution | pH: 7.9 | ||||||||||||||||||||||||||||||
| Specimen | Conc.: 0.3 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: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 90590 / Symmetry type: POINT |
| Atomic model building | Protocol: FLEXIBLE FIT |
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About Yorodumi




Homo sapiens (human)
United States, 4items
Citation
UCSF Chimera























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