|Entry||Database: EMDB / ID: 0587|
|Title||Cryo-EM structure of the human TFIIH core complex: Map sorted for the MAT1 RING domain.|
|Map data||Map sorted for occupancy of the MAT1 RING domain. This map is low-pass filtered to 4.5 Angstroms resolution.|
|Sample||Transcription factor IIH (TFIIH):|
|Source||Homo sapiens (human)|
|Method||single particle reconstruction / cryo EM / 4.1 Å resolution|
|Authors||Greber BJ / Toso D / Fang J / Nogales E|
|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.
|Date||Deposition: Feb 19, 2019 / Header (metadata) release: Feb 13, 2019 / Map release: Mar 13, 2019 / Last update: Mar 27, 2019|
|Structure viewer||EM map: |
Downloads & links
|File||emd_0587.map.gz (map file in CCP4 format, 67109 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.15 Å|
CCP4 map header:
-Entire Transcription factor IIH (TFIIH)
|Entire||Name: Transcription factor IIH (TFIIH) / Number of components: 1|
-Component #1: protein, Transcription factor IIH (TFIIH)
|Protein||Name: Transcription factor IIH (TFIIH) / Recombinant expression: No|
|Mass||Theoretical: 500 kDa|
|Source||Species: Homo sapiens (human)|
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||Specimen conc.: 0.0049 mg/ml / pH: 7.9|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 277 K / Humidity: 100 %|
Details: A thin film of continuous carbon was floated onto Protochips C-flat CF-4/2 holey carbon grids and glow discharged or plasma cleaned before application of 4 uL of sample solution..
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 5 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 43478.0 X (calibrated) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 500.0 - 700.0 nm / Energy filter: GIF Quantum LS|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Image acquisition||Number of digital images: 21437|
Details: Images were collected as dose-fractionated movie frames (33 or 50 frames per exposure).
|Processing||Method: single particle reconstruction / Applied symmetry: C1 (asymmetric) / Number of projections: 81131|
|3D reconstruction||Algorithm: FOURIER SPACE / Software: RELION|
CTF correction: CTF correction during 3D reconstruction in RELION 3.
Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF
Details: The map resolution by FSC=0.143 is 4.1 Angstroms. The map was low-pass filtered to 4.5 Angstroms resolution to improve the interpretability of the region of interest.
-Atomic model buiding
|Modeling #1||Refinement protocol: rigid body / Refinement space: REAL|
Details: Rigid body docking of the NMR ensemble (PDB ID 1G25) into the region of interest.
Input PDB model: 1G25
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