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Yorodumi- PDB-28jm: Cryo-EM structure of the human holo-TFIIH and XPC initial encount... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 28jm | ||||||||||||||||||||||||
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| Title | Cryo-EM structure of the human holo-TFIIH and XPC initial encounter complex | ||||||||||||||||||||||||
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Keywords | DNA BINDING PROTEIN / Nucleotide excision repair / DNA Repair / helicase / transcription factor | ||||||||||||||||||||||||
| Function / homology | Function and homology informationheteroduplex DNA loop binding / nucleotide-excision repair factor 2 complex / pyrimidine dimer repair by nucleotide-excision repair / XPC complex / nucleotide-excision repair complex / MMXD complex / core TFIIH complex portion of holo TFIIH complex / Cytosolic iron-sulfur cluster assembly / DNA damage sensor activity / central nervous system myelin formation ...heteroduplex DNA loop binding / nucleotide-excision repair factor 2 complex / pyrimidine dimer repair by nucleotide-excision repair / XPC complex / nucleotide-excision repair complex / MMXD complex / core TFIIH complex portion of holo TFIIH complex / Cytosolic iron-sulfur cluster assembly / DNA damage sensor activity / central nervous system myelin formation / positive regulation of mitotic recombination / hair cell differentiation / nucleotide-excision repair factor 3 complex / nucleotide-excision repair, preincision complex assembly / hair follicle maturation / ventricular system development / response to auditory stimulus / transcription factor TFIIK complex / CAK-ERCC2 complex / bubble DNA binding / embryonic cleavage / UV protection / regulation of cyclin-dependent protein serine/threonine kinase activity / transcription factor TFIIH core complex / transcription factor TFIIH holo complex / cyclin-dependent protein serine/threonine kinase activator activity / DNA 5'-3' helicase / G protein-coupled receptor internalization / adult heart development / response to UV-B / mitotic intra-S DNA damage checkpoint signaling / nuclear thyroid hormone receptor binding / transcription preinitiation complex / RNA Polymerase I Transcription Termination / UV-damage excision repair / transcription factor TFIID complex / RNA polymerase II general transcription initiation factor activity / erythrocyte maturation / regulation of mitotic cell cycle phase transition / hematopoietic stem cell proliferation / 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 / spinal cord development / ATPase activator activity / 3'-5' DNA helicase activity / DNA 3'-5' helicase / DNA topological change / RNA Polymerase I Transcription Initiation / intrinsic apoptotic signaling pathway by p53 class mediator / regulation of G1/S transition of mitotic cell cycle / hematopoietic stem cell differentiation / embryonic organ development / Tat-mediated elongation of the HIV-1 transcript / Cyclin E associated events during G1/S transition / Formation of HIV-1 elongation complex containing HIV-1 Tat / mismatch repair / SUMOylation of DNA damage response and repair proteins / transcription elongation by RNA polymerase I / response to UV / Cyclin A:Cdk2-associated events at S phase entry / Formation of HIV elongation complex in the absence of HIV Tat / cyclin-dependent protein kinase holoenzyme complex / Cyclin A/B1/B2 associated events during G2/M transition / transcription by RNA polymerase I / site of DNA damage / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / extracellular matrix organization / hormone-mediated signaling pathway / transcription-coupled nucleotide-excision repair / RNA Polymerase II Pre-transcription Events / insulin-like growth factor receptor signaling pathway / positive regulation of smooth muscle cell proliferation / DNA helicase activity / determination of adult lifespan / post-embryonic development / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / TP53 Regulates Transcription of DNA Repair Genes / nucleotide-excision repair / transcription initiation at RNA polymerase II promoter / promoter-specific chromatin binding / RNA Polymerase I Promoter Escape / transcription elongation by RNA polymerase II / chromosome segregation / G1/S transition of mitotic cell cycle / cellular response to gamma radiation / NoRC negatively regulates rRNA expression / response to calcium ion / DNA Damage Recognition in GG-NER Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.29 Å | ||||||||||||||||||||||||
Authors | de Martin Garrido, N. / Haste, C.A.F. / Feng, J. / Cronin, N.B. / Greber, B.J. | ||||||||||||||||||||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: To Be PublishedTitle: Visualisation of stepwise de-repression of TFIIH in global-genome nucleotide excision repair Authors: de Martin Garrido, N. / Haste, C.A.F. / Feng, J. / Cronin, N.B. / Greber, B.J. | ||||||||||||||||||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 28jm.cif.gz | 664.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb28jm.ent.gz | 517.2 KB | Display | PDB format |
| PDBx/mmJSON format | 28jm.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/8j/28jm ftp://data.pdbj.org/pub/pdb/validation_reports/8j/28jm | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 56544MC ![]() 28jsC ![]() 28jvC ![]() 28keC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-Protein , 4 types, 4 molecules ABHI
| #1: Protein | Mass: 91300.711 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ERCC3, XPB, XPBC / Production host: ![]() |
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| #2: Protein | Mass: 88306.305 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ERCC2, XPD, XPDC / Production host: ![]() |
| #8: Protein | Mass: 35873.965 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MNAT1, CAP35, MAT1, RNF66 / Production host: ![]() |
| #9: Protein | Mass: 106142.203 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: XPC, XPCC / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q01831 |
-General transcription factor IIH subunit ... , 5 types, 5 molecules CDEFG
| #3: Protein | Mass: 66403.961 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2H1, BTF2 / Production host: ![]() |
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| #4: Protein | Mass: 52245.156 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2H4 / Production host: ![]() |
| #5: Protein | Mass: 44481.996 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2H2, BTF2P44 / Production host: ![]() |
| #6: Protein | Mass: 34416.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2H3 / Production host: ![]() |
| #7: Protein | Mass: 8060.362 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2H5, C6orf175, TTDA / Production host: ![]() |
-Non-polymers , 2 types, 8 molecules 


| #10: Chemical | ChemComp-SF4 / |
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| #11: Chemical | ChemComp-ZN / |
-Details
| Has ligand of interest | N |
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| Has protein modification | N |
-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: Human holo-TFIIH, XPC complex, and XPA with biotinylated DNA. Type: COMPLEX Details: XPA and DNA are not observed in this reconstruction. Entity ID: #1-#9 / Source: RECOMBINANT | |||||||||||||||||||||||||||||||||||
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| Molecular weight | Value: 0.72682 MDa / Experimental value: NO | |||||||||||||||||||||||||||||||||||
| Source (natural) | Organism: Homo sapiens (human) | |||||||||||||||||||||||||||||||||||
| Source (recombinant) | Organism: ![]() | |||||||||||||||||||||||||||||||||||
| Buffer solution | pH: 7.5 | |||||||||||||||||||||||||||||||||||
| Buffer component |
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| Specimen | Conc.: 0.16 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||||||||||||
| Specimen support | Details: Streptavidin affinity grids / Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R2/2 | |||||||||||||||||||||||||||||||||||
| Vitrification | Instrument: LEICA EM GP / Cryogen name: ETHANE / Humidity: 95 % / Chamber temperature: 293.15 K / Details: Leica EM GP2 |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal magnification: 165000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 600 nm / Cs: 2.7 mm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.29 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 323811 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||||||
| Refinement | Highest resolution: 3.29 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi



Homo sapiens (human)
United Kingdom, 1items
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