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Open data
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Basic information
Entry | Database: PDB / ID: 6mzm | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Title | Human TFIID bound to promoter DNA and TFIIA | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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![]() | transcription/dna / Transcription / DNA / Nuclear / transcription-dna complex | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Function / homology | ![]() negative regulation of MHC class I biosynthetic process / spermine transport / SAGA complex assembly / lateral mesodermal cell differentiation / DNA-templated transcription open complex formation / allantois development / pre-snoRNP complex / positive regulation of androgen receptor signaling pathway / TFIIH-class transcription factor complex binding / negative regulation of protein autoubiquitination ...negative regulation of MHC class I biosynthetic process / spermine transport / SAGA complex assembly / lateral mesodermal cell differentiation / DNA-templated transcription open complex formation / allantois development / pre-snoRNP complex / positive regulation of androgen receptor signaling pathway / TFIIH-class transcription factor complex binding / negative regulation of protein autoubiquitination / transcription factor TFTC complex / RNA polymerase I general transcription initiation factor activity / regulation of cell cycle G1/S phase transition / RNA polymerase transcription factor SL1 complex / SLIK (SAGA-like) complex / histone H4K16ac reader activity / negative regulation of MHC class II biosynthetic process / RNA polymerase III general transcription initiation factor activity / : / RNA polymerase I core promoter sequence-specific DNA binding / hepatocyte differentiation / positive regulation of response to cytokine stimulus / maintenance of protein location in nucleus / 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 / C2H2 zinc finger domain binding / RNA Polymerase III Abortive And Retractive Initiation / female germ cell nucleus / male pronucleus / female pronucleus / negative regulation of signal transduction by p53 class mediator / RNA polymerase II general transcription initiation factor binding / nuclear vitamin D receptor binding / RNA polymerase binding / nuclear thyroid hormone receptor binding / regulation of fat cell differentiation / box C/D snoRNP assembly / limb development / SAGA complex / cellular response to ATP / RNA Polymerase I Transcription Termination / transcription preinitiation complex / response to L-glutamate / inner cell mass cell proliferation / RNA polymerase II general transcription initiation factor activity / transcription factor TFIID complex / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / 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 / regulation of RNA splicing / transcription initiation at RNA polymerase I promoter / ubiquitin conjugating enzyme activity / aryl hydrocarbon receptor binding / negative regulation of cell cycle / histone acetyltransferase activity / TFIIB-class transcription factor binding / RNA Polymerase I Transcription Initiation / P-TEFb complex binding / MLL1 complex / RNA polymerase II transcribes snRNA genes / negative regulation of ubiquitin-dependent protein catabolic process / transcription by RNA polymerase III / positive regulation of transcription initiation by RNA polymerase II / embryonic placenta development / somitogenesis / RNA polymerase II core promoter sequence-specific DNA binding / regulation of DNA repair / core promoter sequence-specific DNA binding / transcription regulator inhibitor activity / histone acetyltransferase / RNA polymerase II preinitiation complex assembly / ovarian follicle development / positive regulation of intrinsic apoptotic signaling pathway / negative regulation of protein kinase activity / estrogen receptor signaling pathway / RNA Polymerase II Pre-transcription Events / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / response to interleukin-1 / TBP-class protein binding / male germ cell nucleus / SIRT1 negatively regulates rRNA expression / regulation of signal transduction by p53 class mediator / nuclear estrogen receptor binding / nuclear receptor binding / transcription initiation at RNA polymerase II promoter / RNA Polymerase I Promoter Escape / DNA-templated transcription initiation / mRNA transcription by RNA polymerase II / promoter-specific chromatin binding / G1/S transition of mitotic cell cycle / euchromatin Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Biological species | ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.5 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
![]() | Patel, A.B. / Louder, R.K. / Greber, B.J. / Grunberg, S. / Luo, J. / Fang, J. / Liu, Y. / Ranish, J. / Hahn, S. / Nogales, E. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure of human TFIID and mechanism of TBP loading onto promoter DNA. Authors: Avinash B Patel / Robert K Louder / Basil J Greber / Sebastian Grünberg / Jie Luo / Jie Fang / Yutong Liu / Jeff Ranish / Steve Hahn / Eva Nogales / ![]() Abstract: The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and ...The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and initiating PIC assembly. We used cryo-electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box-binding protein (TBP) loading onto promoter DNA. Our structural analysis revealed five structural states of TFIID in the presence of TFIIA and promoter DNA, showing that the initial binding of TFIID to the downstream promoter positions the upstream DNA and facilitates scanning of TBP for a TATA box and the subsequent engagement of the promoter. Our findings provide a mechanistic model for the specific loading of TBP by TFIID onto the promoter. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
History |
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Structure visualization
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 779.3 KB | Display | ![]() |
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PDB format | ![]() | 560.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.3 MB | Display | |
Data in XML | ![]() | 103.4 KB | Display | |
Data in CIF | ![]() | 159.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9306MC ![]() 9298C ![]() 9299C ![]() 9300C ![]() 9301C ![]() 9302C ![]() 9305C ![]() 6mzcC ![]() 6mzdC ![]() 6mzlC C: citing same article ( M: map data used to model this data |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Transcription initiation factor TFIID subunit ... , 11 types, 11 molecules ABDGHIJKLOR
#1: Protein | Mass: 57193.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: Protein | Mass: 137159.984 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#3: Protein | Mass: 104052.086 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#4: Protein | Mass: 85785.164 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#5: Protein | Mass: 72749.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#6: Protein | Mass: 72365.836 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#7: Protein | Mass: 40325.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#8: Protein | Mass: 32975.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#9: Protein | Mass: 28830.689 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#10: Protein | Mass: 21731.248 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
#11: Protein | Mass: 17948.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 2 types, 2 molecules TZ
#12: Protein | Mass: 37729.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#17: Protein | Mass: 20272.906 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-DNA chain , 2 types, 2 molecules UV
#13: DNA chain | Mass: 24498.586 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
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#14: DNA chain | Mass: 24854.842 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() |
-Transcription initiation factor IIA subunit ... , 2 types, 2 molecules WX
#15: Protein | Mass: 10675.194 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#16: Protein | Mass: 11275.824 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Details
Has protein modification | N |
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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: General transcription factor IID / Type: COMPLEX / Entity ID: all / Source: NATURAL | ||||||||||||||||||||||||||||
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Source (natural) | Organism: ![]() | ||||||||||||||||||||||||||||
Buffer solution | pH: 7.9 | ||||||||||||||||||||||||||||
Buffer component |
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Specimen | Conc.: 0.2 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 % / Chamber temperature: 277.15 K / Details: BT 4s; BF 15N |
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Electron microscopy imaging
Microscopy | Model: FEI TITAN |
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Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Cs: 2.7 mm / C2 aperture diameter: 50 µm |
Specimen holder | Cryogen: NITROGEN Specimen holder model: GATAN 626 SINGLE TILT LIQUID NITROGEN CRYO TRANSFER HOLDER |
Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
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Processing
Software | Name: PHENIX / Version: 1.14_3211: / Classification: refinement | ||||||||||||||||||||||||
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EM software |
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 7.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 25180 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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