+Open data
-Basic information
Entry | Database: PDB / ID: 6nmi | |||||||||||||||
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Title | Cryo-EM structure of the human TFIIH core complex | |||||||||||||||
Components |
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Keywords | TRANSCRIPTION / DNA repair / helicase / multiprotein complex | |||||||||||||||
Function / homology | Function and homology information MMXD complex / core TFIIH complex portion of holo TFIIH complex / positive regulation of DNA helicase activity / negative regulation of DNA helicase activity / Cytosolic iron-sulfur cluster assembly / nucleotide-excision repair, DNA duplex unwinding / central nervous system myelin formation / positive regulation of mitotic recombination / hair follicle maturation / hair cell differentiation ...MMXD complex / core TFIIH complex portion of holo TFIIH complex / positive regulation of DNA helicase activity / negative regulation of DNA helicase activity / Cytosolic iron-sulfur cluster assembly / nucleotide-excision repair, DNA duplex unwinding / central nervous system myelin formation / positive regulation of mitotic recombination / hair follicle maturation / hair cell differentiation / ventricular system development / nucleotide-excision repair factor 3 complex / cyclin-dependent protein kinase activating kinase holoenzyme complex / nucleotide-excision repair, preincision complex assembly / UV protection / CAK-ERCC2 complex / transcription factor TFIIK complex / embryonic cleavage / adult heart development / G protein-coupled receptor internalization / transcription factor TFIIH core complex / cyclin-dependent protein serine/threonine kinase activator activity / transcription factor TFIIH holo complex / nuclear thyroid hormone receptor binding / transcription preinitiation complex / RNA Polymerase I Transcription Termination / regulation of mitotic cell cycle phase transition / hematopoietic stem cell proliferation / 3'-5' DNA helicase activity / spinal cord development / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / mRNA Capping / bone mineralization / 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 / erythrocyte maturation / regulation of cyclin-dependent protein serine/threonine kinase activity / ATPase activator activity / regulation of G1/S transition of mitotic cell cycle / RNA Polymerase I Transcription Initiation / transcription elongation by RNA polymerase I / DNA topological change / transcription factor TFIID complex / intrinsic apoptotic signaling pathway by p53 class mediator / RNA polymerase II general transcription initiation factor activity / transcription by RNA polymerase I / hematopoietic stem cell differentiation / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / embryonic organ development / transcription-coupled nucleotide-excision repair / Formation of HIV elongation complex in the absence of HIV Tat / Cyclin E associated events during G1/S transition / RNA Polymerase II Transcription Elongation / Cyclin A/B1/B2 associated events during G2/M transition / Formation of RNA Pol II elongation complex / response to UV / Cyclin A:Cdk2-associated events at S phase entry / RNA Polymerase II Pre-transcription Events / DNA helicase activity / hormone-mediated signaling pathway / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / extracellular matrix organization / insulin-like growth factor receptor signaling pathway / post-embryonic development / chromosome segregation / determination of adult lifespan / transcription elongation by RNA polymerase II / promoter-specific chromatin binding / transcription initiation at RNA polymerase II promoter / nucleotide-excision repair / RNA Polymerase I Promoter Escape / TP53 Regulates Transcription of DNA Repair Genes / positive regulation of smooth muscle cell proliferation / NoRC negatively regulates rRNA expression / protein localization / multicellular organism growth / Dual Incision in GG-NER / G1/S transition of mitotic cell cycle / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / cellular response to gamma radiation / Formation of TC-NER Pre-Incision Complex / Formation of Incision Complex in GG-NER / response to calcium ion / spindle / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / Cyclin D associated events in G1 / protein-macromolecule adaptor activity / RUNX1 regulates transcription of genes involved in differentiation of HSCs / 4 iron, 4 sulfur cluster binding / 5'-3' DNA helicase activity Similarity search - Function | |||||||||||||||
Biological species | Homo sapiens (human) | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||||||||
Authors | Greber, B.J. / Toso, D. / Fang, J. / Nogales, E. | |||||||||||||||
Funding support | United States, Switzerland, 4items
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Citation | Journal: Elife / Year: 2019 Title: The complete structure of the human TFIIH core complex. Authors: Basil J Greber / Daniel B Toso / Jie Fang / Eva Nogales / Abstract: Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair. The TFIIH core complex is ...Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair. The TFIIH core complex is sufficient for its repair functions and harbors the XPB and XPD DNA-dependent ATPase/helicase subunits, which are affected by human disease mutations. Transcription initiation additionally requires the CdK activating kinase subcomplex. Previous structural work has provided only partial insight into the architecture of TFIIH and its interactions within transcription pre-initiation complexes. Here, we present the complete structure of the human TFIIH core complex, determined by phase-plate cryo-electron microscopy at 3.7 Å resolution. The structure uncovers the molecular basis of TFIIH assembly, revealing how the recruitment of XPB by p52 depends on a pseudo-symmetric dimer of homologous domains in these two proteins. The structure also suggests a function for p62 in the regulation of XPD, and allows the mapping of previously unresolved human disease mutations. | |||||||||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 6nmi.cif.gz | 553.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6nmi.ent.gz | 452.3 KB | Display | PDB format |
PDBx/mmJSON format | 6nmi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nm/6nmi ftp://data.pdbj.org/pub/pdb/validation_reports/nm/6nmi | HTTPS FTP |
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-Related structure data
Related structure data | 0452MC 0587C 0588C 0589C 0602C 0603C 0604C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | |
EM raw data | EMPIAR-10430 (Title: Phase-plate cryo-EM of human TFIIH / Data size: 9.2 TB Data #1: Unaligned movies of human TFIIH, using the Volta phase plate, dataset 1 [micrographs - multiframe] Data #2: Unaligned movies of human TFIIH, using the Volta phase plate, dataset 2 [micrographs - multiframe] Data #3: Unaligned movies of human TFIIH, using the Volta phase plate, dataset 3 [micrographs - multiframe] Data #4: Unaligned movies of human TFIIH, using the Volta phase plate, dataset 4 [micrographs - multiframe] Data #5: Unaligned movies of human TFIIH, using the Volta phase plate, dataset 5 [micrographs - multiframe] Data #6: Unaligned movies of human TFIIH, using the Volta phase plate, dataset 6 [micrographs - multiframe]) |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-General transcription and DNA repair factor IIH helicase subunit ... , 2 types, 2 molecules AB
#1: Protein | Mass: 74233.492 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: P19447*PLUS, DNA helicase |
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#2: Protein | Mass: 86417.766 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: P18074*PLUS |
-General transcription factor IIH subunit ... , 5 types, 5 molecules CDEFG
#3: Protein | Mass: 57789.000 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: P32780*PLUS |
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#4: Protein | Mass: 52245.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: Q92759 |
#5: Protein | Mass: 39609.098 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: Q13888*PLUS |
#6: Protein | Mass: 34416.008 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: Q13889 |
#7: Protein | Mass: 8060.362 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: Q6ZYL4 |
-Protein , 1 types, 1 molecules H
#8: Protein | Mass: 35873.965 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HeLa / References: UniProt: P51948 |
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-Non-polymers , 2 types, 7 molecules
#9: Chemical | ChemComp-SF4 / |
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#10: Chemical | ChemComp-ZN / |
-Details
Sequence details | The full sequence for General transcription factor IIH subunit 1, p62 ...The full sequence for General transcription factor IIH subunit 1, p62 MATSSEEVLL |
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