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Open data
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Basic information
| Entry | Database: PDB / ID: 7egh | ||||||
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| Title | TFIID lobe C subcomplex | ||||||
Components |
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Keywords | TRANSCRIPTION / TFIID / preinitiation complex / core promoter / transcription initiation | ||||||
| Function / homology | Function and homology informationnegative regulation of MHC class I biosynthetic process / spermine transport / DNA-templated transcription open complex formation / positive regulation of androgen receptor signaling pathway / TFIIH-class transcription factor complex binding / negative regulation of protein autoubiquitination / negative regulation of MHC class II biosynthetic process / transcription factor TFTC complex / RNA polymerase I general transcription initiation factor activity / regulation of cell cycle G1/S phase transition ...negative regulation of MHC class I biosynthetic process / spermine transport / DNA-templated transcription open complex formation / positive regulation of androgen receptor signaling pathway / TFIIH-class transcription factor complex binding / negative regulation of protein autoubiquitination / negative regulation of MHC class II biosynthetic process / transcription factor TFTC complex / RNA polymerase I general transcription initiation factor activity / regulation of cell cycle G1/S phase transition / SLIK (SAGA-like) complex / histone H4K16ac reader activity / maintenance of protein location in nucleus / RNA polymerase II general transcription initiation factor binding / nuclear vitamin D receptor binding / nuclear thyroid hormone receptor binding / regulation of fat cell differentiation / SAGA complex / inner cell mass cell proliferation / RNA polymerase II general transcription initiation factor activity / transcription factor TFIID complex / histone acetyltransferase binding / 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 / midbrain development / cellular response to ATP / negative regulation of signal transduction by p53 class mediator / negative regulation of cell cycle / transcription initiation at RNA polymerase I promoter / aryl hydrocarbon receptor binding / ubiquitin conjugating enzyme activity / P-TEFb complex binding / MLL1 complex / RNA polymerase II transcribes snRNA genes / negative regulation of ubiquitin-dependent protein catabolic process / positive regulation of transcription initiation by RNA polymerase II / histone acetyltransferase activity / RNA polymerase II core promoter sequence-specific DNA binding / regulation of DNA repair / negative regulation of protein kinase activity / RNA polymerase II preinitiation complex assembly / transcription regulator inhibitor activity / histone acetyltransferase / positive regulation of intrinsic apoptotic signaling pathway / estrogen receptor signaling pathway / RNA Polymerase II Pre-transcription Events / TBP-class protein binding / regulation of signal transduction by p53 class mediator / nuclear receptor binding / male germ cell nucleus / transcription initiation at RNA polymerase II promoter / DNA-templated transcription initiation / mRNA transcription by RNA polymerase II / G2/M transition of mitotic cell cycle / protein polyubiquitination / cellular response to UV / p53 binding / kinase activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / protein autophosphorylation / chromatin organization / ubiquitin-dependent protein catabolic process / transcription regulator complex / Regulation of TP53 Activity through Phosphorylation / DNA-binding transcription factor binding / sequence-specific DNA binding / RNA polymerase II-specific DNA-binding transcription factor binding / transcription by RNA polymerase II / cell differentiation / transcription coactivator activity / non-specific serine/threonine protein kinase / protein kinase activity / transcription cis-regulatory region binding / protein stabilization / positive regulation of apoptotic process / protein heterodimerization activity / negative regulation of cell population proliferation / negative regulation of gene expression / protein serine kinase activity / negative regulation of DNA-templated transcription / protein serine/threonine kinase activity / apoptotic process / DNA damage response / chromatin binding / regulation of transcription by RNA polymerase II / chromatin / positive regulation of DNA-templated transcription / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / nucleoplasm / ATP binding / nucleus Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.04 Å | ||||||
Authors | Chen, X. / Wu, Z. / Li, J. / Zhao, D. / Xu, Y. | ||||||
Citation | Journal: Science / Year: 2021Title: Structural insights into preinitiation complex assembly on core promoters. Authors: Xizi Chen / Yilun Qi / Zihan Wu / Xinxin Wang / Jiabei Li / Dan Zhao / Haifeng Hou / Yan Li / Zishuo Yu / Weida Liu / Mo Wang / Yulei Ren / Ze Li / Huirong Yang / Yanhui Xu / ![]() Abstract: Transcription factor IID (TFIID) recognizes core promoters and supports preinitiation complex (PIC) assembly for RNA polymerase II (Pol II)-mediated eukaryotic transcription. We determined the ...Transcription factor IID (TFIID) recognizes core promoters and supports preinitiation complex (PIC) assembly for RNA polymerase II (Pol II)-mediated eukaryotic transcription. We determined the structures of human TFIID-based PIC in three stepwise assembly states and revealed two-track PIC assembly: stepwise promoter deposition to Pol II and extensive modular reorganization on track I (on TATA-TFIID-binding element promoters) versus direct promoter deposition on track II (on TATA-only and TATA-less promoters). The two tracks converge at an ~50-subunit holo PIC in identical conformation, whereby TFIID stabilizes PIC organization and supports loading of cyclin-dependent kinase (CDK)-activating kinase (CAK) onto Pol II and CAK-mediated phosphorylation of the Pol II carboxyl-terminal domain. Unexpectedly, TBP of TFIID similarly bends TATA box and TATA-less promoters in PIC. Our study provides structural visualization of stepwise PIC assembly on highly diversified promoters. | ||||||
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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 | 7egh.cif.gz | 521.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7egh.ent.gz | 381.9 KB | Display | PDB format |
| PDBx/mmJSON format | 7egh.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7egh_validation.pdf.gz | 683.1 KB | Display | wwPDB validaton report |
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| Full document | 7egh_full_validation.pdf.gz | 690.1 KB | Display | |
| Data in XML | 7egh_validation.xml.gz | 57.4 KB | Display | |
| Data in CIF | 7egh_validation.cif.gz | 93.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eg/7egh ftp://data.pdbj.org/pub/pdb/validation_reports/eg/7egh | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 31117MC ![]() 7edxC ![]() 7eg7C ![]() 7eg8C ![]() 7eg9C ![]() 7egaC ![]() 7egbC ![]() 7egcC ![]() 7egdC ![]() 7egeC ![]() 7egfC ![]() 7eggC ![]() 7egiC ![]() 7egjC 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
-Transcription initiation factor TFIID subunit ... , 5 types, 6 molecules ABFfGH
| #1: Protein | Mass: 212956.172 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TAF1, BA2R, CCG1, CCGS, TAF2A / Production host: Homo sapiens (human)References: UniProt: P21675, histone acetyltransferase, non-specific serine/threonine protein kinase | ||||
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| #2: Protein | Mass: 137159.984 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TAF2, CIF150, TAF2B / Production host: Homo sapiens (human) / References: UniProt: Q6P1X5 | ||||
| #3: Protein | Mass: 72749.297 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TAF6, TAF2E, TAFII70 / Production host: Homo sapiens (human) / References: UniProt: P49848#4: Protein | | Mass: 40325.117 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TAF7, TAF2F, TAFII55 / Production host: Homo sapiens (human) / References: UniProt: Q15545#5: Protein | | Mass: 34304.359 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TAF8, TAFII43, TBN / Production host: Homo sapiens (human) / References: UniProt: Q7Z7C8 |
-DNA chain , 2 types, 2 molecules XY
| #6: DNA chain | Mass: 22317.238 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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| #7: DNA chain | Mass: 28814.336 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
-Details
| Has protein modification | 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 |
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Sample preparation
| Component | Name: TFIID lobe C subcomplex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Molecular weight | Units: KILODALTONS/NANOMETER / Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.9 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: GOLD |
| Vitrification | Instrument: FEI VITROBOT MARK IV / 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 / Cs: 2.7 mm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 50 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
| Image scans | Movie frames/image: 32 |
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Processing
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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| 3D reconstruction | Resolution: 3.04 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 121285 / Symmetry type: POINT |
| Atomic model building | Protocol: AB INITIO MODEL / Space: REAL |
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