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Open data
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Basic information
| Entry | Database: PDB / ID: 6o9l | ||||||
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| Title | Human holo-PIC in the closed state | ||||||
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Keywords | TRANSCRIPTION/DNA / Transcription initiation / Molecular dynamics / Gene regulation / Community network analysis / Global protein dynamics / RNA polymerase / TRANSCRIPTION-DNA complex | ||||||
| Function / homology | Function and homology informationmicrofibril binding / MMXD complex / core TFIIH complex portion of holo TFIIH complex / Cytosolic iron-sulfur cluster assembly / central nervous system myelin formation / RNA Polymerase III Chain Elongation / positive regulation of core promoter binding / RNA polymerase II core complex assembly / RNA polymerase II CTD heptapeptide repeat S5 kinase activity / positive regulation of mitotic recombination ...microfibril binding / MMXD complex / core TFIIH complex portion of holo TFIIH complex / Cytosolic iron-sulfur cluster assembly / central nervous system myelin formation / RNA Polymerase III Chain Elongation / positive regulation of core promoter binding / RNA polymerase II core complex assembly / RNA polymerase II CTD heptapeptide repeat S5 kinase activity / positive regulation of mitotic recombination / RNA Polymerase III Transcription Termination / hair cell differentiation / hair follicle maturation / transcription factor TFIIE complex / nucleotide-excision repair factor 3 complex / RNA polymerase transcription factor SL1 complex / nucleotide-excision repair, preincision complex assembly / meiotic sister chromatid cohesion / phosphatase activator activity / ventricular system development / snRNA transcription by RNA polymerase II / CAK-ERCC2 complex / RNA polymerase III general transcription initiation factor activity / TFIIF-class transcription factor complex binding / regulation of transcription by RNA polymerase I / transcription factor TFIIK complex / 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 / embryonic cleavage / DNA 5'-3' helicase / 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 / adult heart development / female germ cell nucleus / UV protection / RNA Polymerase III Abortive And Retractive Initiation / regulation of cyclin-dependent protein serine/threonine kinase activity / Cytosolic sensors of pathogen-associated DNA / transcription factor TFIIH core complex / transcription factor TFIIH holo complex / male pronucleus / G protein-coupled receptor internalization / cyclin-dependent protein serine/threonine kinase activator activity / female pronucleus / germinal vesicle / RNA polymerase II general transcription initiation factor binding / nuclear thyroid hormone receptor binding / [RNA-polymerase]-subunit kinase / Abortive elongation of HIV-1 transcript in the absence of Tat / transcription preinitiation complex / FGFR2 alternative splicing / RNA Polymerase I Transcription Termination / cyclin-dependent protein serine/threonine kinase regulator activity / MicroRNA (miRNA) biogenesis / Viral Messenger RNA Synthesis / Signaling by FGFR2 IIIa TM / DNA 3'-5' helicase / regulation of mitotic cell cycle phase transition / LRR domain binding / protein acetylation / RNA polymerase II general transcription initiation factor activity / transcription factor TFIID complex / cell division site / erythrocyte maturation / 3'-5' DNA helicase activity / hematopoietic stem cell proliferation / spinal cord development / 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 / bone mineralization / mRNA Capping / mRNA Splicing - Minor Pathway / PIWI-interacting RNA (piRNA) biogenesis / aryl hydrocarbon receptor binding / viral transcription / RNA polymerase II complex binding / TFIIB-class transcription factor binding / ATPase activator activity / DNA topological change / intrinsic apoptotic signaling pathway by p53 class mediator / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase I Transcription Initiation / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / nuclear-transcribed mRNA catabolic process / regulation of G1/S transition of mitotic cell cycle Similarity search - Function | ||||||
| Biological species | Homo sapiens (human)synthetic construct (others) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.2 Å | ||||||
Authors | Yan, C.L. / Dodd, T. / He, Y. / Tainer, J.A. / Tsutakawa, S.E. / Ivanov, I. | ||||||
| Funding support | United States, 1items
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Citation | Journal: Nature / Year: 2016Title: Structure of promoter-bound TFIID and model of human pre-initiation complex assembly. Authors: Robert K Louder / Yuan He / José Ramón López-Blanco / Jie Fang / Pablo Chacón / Eva Nogales / ![]() Abstract: The general transcription factor IID (TFIID) plays a central role in the initiation of RNA polymerase II (Pol II)-dependent transcription by nucleating pre-initiation complex (PIC) assembly at the ...The general transcription factor IID (TFIID) plays a central role in the initiation of RNA polymerase II (Pol II)-dependent transcription by nucleating pre-initiation complex (PIC) assembly at the core promoter. TFIID comprises the TATA-binding protein (TBP) and 13 TBP-associated factors (TAF1-13), which specifically interact with a variety of core promoter DNA sequences. Here we present the structure of human TFIID in complex with TFIIA and core promoter DNA, determined by single-particle cryo-electron microscopy at sub-nanometre resolution. All core promoter elements are contacted by subunits of TFIID, with TAF1 and TAF2 mediating major interactions with the downstream promoter. TFIIA bridges the TBP-TATA complex with lobe B of TFIID. We also present the cryo-electron microscopy reconstruction of a fully assembled human TAF-less PIC. Superposition of common elements between the two structures provides novel insights into the general role of TFIID in promoter recognition, PIC assembly, and transcription initiation. | ||||||
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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 | 6o9l.cif.gz | 1.8 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb6o9l.ent.gz | 1.4 MB | Display | PDB format |
| PDBx/mmJSON format | 6o9l.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/o9/6o9l ftp://data.pdbj.org/pub/pdb/validation_reports/o9/6o9l | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 3307M ![]() 6o9mC 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 ... , 8 types, 8 molecules ABCDEGIK
| #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 |
| #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 |
| #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 |
| #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 |
-DNA-directed RNA polymerases I, II, and III subunit ... , 4 types, 4 molecules FHJL
| #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 |
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| #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 |
| #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 |
| #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 natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P52655 |
| #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 , 6 types, 6 molecules PQU389
| #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 natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P23193 |
| #25: Protein | Mass: 35873.965 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P51948 |
| #30: Protein | Mass: 39090.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)References: UniProt: P50613, cyclin-dependent kinase, [RNA-polymerase]-subunit kinase |
| #31: Protein | Mass: 37695.473 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P51946 |
-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: ![]() |
-TFIIH basal transcription factor complex helicase ... , 2 types, 2 molecules 07
| #22: Protein | Mass: 87021.078 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ERCC2, XPD, XPDC / Production host: ![]() |
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| #29: 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 |
-General transcription factor IIH subunit ... , 5 types, 5 molecules 12456
| #23: Protein | Mass: 62116.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P32780 |
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| #24: Protein | Mass: 52245.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q92759 |
| #26: Protein | Mass: 34416.008 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q13889 |
| #27: Protein | Mass: 8060.362 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q6ZYL4 |
| #28: Protein | Mass: 44481.996 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q13888 |
-DNA chain , 2 types, 2 molecules XY
| #32: DNA chain | Mass: 20214.896 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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| #33: DNA chain | Mass: 19867.658 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Non-polymers , 3 types, 20 molecules 




| #34: Chemical | | #35: Chemical | ChemComp-ZN / #36: Chemical | ChemComp-SF4 / | |
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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: holo-PIC in the closed state / Type: COMPLEX / Entity ID: #1-#33 / Source: NATURAL |
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| Source (natural) | Organism: Homo sapiens (human) |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid type: C-flat |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE |
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Electron microscopy imaging
| Microscopy | Model: FEI TITAN |
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| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 46 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
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| 3D reconstruction | Resolution: 7.2 Å / Num. of particles: 24290 | |||||||||||||||||||||||||
| Atomic model building | Protocol: OTHER / Space: REAL Details: Initial model assembled from high-resolution structures and homology models, subsequently rebuilt in COOT, refined into the Cryo-EM map using Phenix and fully validated. |
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Homo sapiens (human)
United States, 1items
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UCSF Chimera









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