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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 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components |
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Keywords | transcription/dna / Transcription / DNA / Nuclear / transcription-dna complex | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationnegative 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 / 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 / RNA polymerase transcription factor SL1 complex / SLIK (SAGA-like) complex / histone H4K16ac reader activity / 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 / 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 / maintenance of protein location in nucleus / C2H2 zinc finger domain binding / female germ cell nucleus / RNA Polymerase III Abortive And Retractive Initiation / male pronucleus / female pronucleus / 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 / limb development / box C/D snoRNP assembly / SAGA complex / transcription preinitiation complex / RNA Polymerase I Transcription Termination / 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 / midbrain development / 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 / cellular response to ATP / negative regulation of signal transduction by p53 class mediator / regulation of RNA splicing / transcription initiation at RNA polymerase I promoter / negative regulation of cell cycle / aryl hydrocarbon receptor binding / ubiquitin conjugating enzyme activity / TFIIB-class transcription factor binding / P-TEFb complex binding / RNA Polymerase I Transcription Initiation / MLL1 complex / transcription by RNA polymerase III / RNA polymerase II transcribes snRNA genes / negative regulation of ubiquitin-dependent protein catabolic process / positive regulation of transcription initiation by RNA polymerase II / embryonic placenta development / somitogenesis / histone acetyltransferase activity / RNA polymerase II core promoter sequence-specific DNA binding / 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 / ovarian follicle development / positive regulation of intrinsic apoptotic signaling pathway / estrogen receptor signaling pathway / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / RNA Polymerase II Pre-transcription Events / response to interleukin-1 / TBP-class protein binding / regulation of signal transduction by p53 class mediator / nuclear estrogen receptor binding / nuclear receptor binding / SIRT1 negatively regulates rRNA expression / male germ cell nucleus / transcription initiation at RNA polymerase II promoter / promoter-specific chromatin binding / RNA Polymerase I Promoter Escape / DNA-templated transcription initiation / mRNA transcription by RNA polymerase II / G1/S transition of mitotic cell cycle / euchromatin / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 7.5 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Authors | 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 | United States, 2items
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Citation | Journal: Science / Year: 2018Title: 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. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Structure visualization
| Movie |
Movie viewer |
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6mzm.cif.gz | 779.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6mzm.ent.gz | 560.1 KB | Display | PDB format |
| PDBx/mmJSON format | 6mzm.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6mzm_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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| Full document | 6mzm_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | 6mzm_validation.xml.gz | 103.4 KB | Display | |
| Data in CIF | 6mzm_validation.cif.gz | 159.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mz/6mzm ftp://data.pdbj.org/pub/pdb/validation_reports/mz/6mzm | 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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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) Homo sapiens (human) / References: UniProt: P21675*PLUS |
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| #2: Protein | Mass: 137159.984 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q6P1X5 |
| #3: Protein | Mass: 104052.086 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O00268 |
| #4: Protein | Mass: 85785.164 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15542 |
| #5: Protein | Mass: 72749.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P49848 |
| #6: Protein | Mass: 72365.836 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P49848 |
| #7: Protein | Mass: 40325.117 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q15545 |
| #8: Protein | Mass: 32975.344 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q7Z7C8 |
| #9: Protein | Mass: 28830.689 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q16594 |
| #10: Protein | Mass: 21731.248 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q12962 |
| #11: Protein | Mass: 17948.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: Q16514 |
-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) Homo sapiens (human) / References: UniProt: P20226 |
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| #17: Protein | Mass: 20272.906 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
-DNA chain , 2 types, 2 molecules UV
| #13: DNA chain | Mass: 24498.586 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
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| #14: DNA chain | Mass: 24854.842 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
-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.) Homo sapiens (human) / Gene: GTF2A1, TF2A1 / Production host: ![]() |
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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.) Homo sapiens (human) / Gene: GTF2A2, TF2A2 / Production host: ![]() |
-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: Homo sapiens (human) / Strain: HeLa | ||||||||||||||||||||||||||||
| Buffer solution | pH: 7.9 | ||||||||||||||||||||||||||||
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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: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| 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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About Yorodumi




Homo sapiens (human)
United States, 2items
Citation
UCSF Chimera














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