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Open data
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Basic information
| Entry | Database: PDB / ID: 9ynw | ||||||
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| Title | Tra1, Core and minimal HAT modules of ctSAGA, composite. | ||||||
Components |
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Keywords | TRANSCRIPTION / ctSAGA complex / Histone Acetyl Transferase (HAT) Module / Tra1 module and Core module | ||||||
| Function / homology | Function and homology informationSAGA-type complex / RITS complex assembly / regulatory ncRNA-mediated heterochromatin formation / SLIK (SAGA-like) complex / histone H3 acetyltransferase activity / SAGA complex / RNA polymerase II general transcription initiation factor activity / transcription factor TFIID complex / NuA4 histone acetyltransferase complex / histone acetyltransferase complex ...SAGA-type complex / RITS complex assembly / regulatory ncRNA-mediated heterochromatin formation / SLIK (SAGA-like) complex / histone H3 acetyltransferase activity / SAGA complex / RNA polymerase II general transcription initiation factor activity / transcription factor TFIID complex / NuA4 histone acetyltransferase complex / histone acetyltransferase complex / histone acetyltransferase / RNA polymerase II preinitiation complex assembly / translation initiation factor activity / TBP-class protein binding / transcription coregulator activity / transcription initiation at RNA polymerase II promoter / promoter-specific chromatin binding / chromatin organization / transcription by RNA polymerase II / transcription coactivator activity / chromatin remodeling / protein heterodimerization activity / DNA repair / chromatin binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / structural molecule activity / positive regulation of transcription by RNA polymerase II / DNA binding / zinc ion binding / nucleus Similarity search - Function | ||||||
| Biological species | Thermochaetoides thermophila (fungus) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||
Authors | Mattoo, R.U.H. / Chen, D.H. / Bushnell, D.A. / Tamir, S. / Kornberg, R.D. | ||||||
| Funding support | United States, 1items
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Citation | Journal: Mol Cell / Year: 2025Title: Structure of the transcriptional co-activator SAGA complex, including the histone acetyltransferase module. Authors: Rayees U H Mattoo / Dong-Hua Chen / David A Bushnell / Sagi Tamir / Roger D Kornberg / ![]() Abstract: The Spt-Ada-Gcn5 acetyltransferase (SAGA) complex, a 1.8 MDa multi-subunit assembly comprising 19 subunits, is required for RNA polymerase II transcription in eukaryotes. The complex consists of four ...The Spt-Ada-Gcn5 acetyltransferase (SAGA) complex, a 1.8 MDa multi-subunit assembly comprising 19 subunits, is required for RNA polymerase II transcription in eukaryotes. The complex consists of four modules: transcription-associated protein 1 (Tra1), core, deubiquitination (DUB), and histone acetyltransferase (HAT). Although the structures of the Tra1, core, and DUB modules have been determined, the overall architecture of the HAT module remained elusive due to its inherent flexibility. To address this, we conducted cryo-electron microscopy (cryo-EM) analyses on SAGA purified from the thermophilic fungus Chaetomium thermophilum, yielding structures of Tra1 and core modules at 2.6 Å and three of the four HAT subunits at 3.7 Å. The structure of the HAT module was informative about the aspects of histone acetylation and the interface of HAT-core modules, contradicting earlier AlphaFold predictions. Our structure-guided genetic and biochemical analyses confirmed the roles of Ada1 and Spt7 in anchoring the HAT module within the SAGA complex. | ||||||
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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 | 9ynw.cif.gz | 3.5 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9ynw.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9ynw.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9ynw_validation.pdf.gz | 1 MB | Display | wwPDB validaton report |
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| Full document | 9ynw_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | 9ynw_validation.xml.gz | 164.2 KB | Display | |
| Data in CIF | 9ynw_validation.cif.gz | 261.8 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yn/9ynw ftp://data.pdbj.org/pub/pdb/validation_reports/yn/9ynw | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 73236MC ![]() 9ynuC ![]() 9ynvC ![]() 9yolC ![]() 9yoqC ![]() 9yzyC 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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Components
-Protein , 6 types, 6 molecules ABFQMN
| #1: Protein | Mass: 444670.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S842 |
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| #2: Protein | Mass: 128449.367 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0RYM2 |
| #6: Protein | Mass: 28834.281 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) |
| #10: Protein | Mass: 137082.672 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S6A1 |
| #12: Protein | Mass: 58866.070 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S7B2 |
| #13: Protein | Mass: 46983.691 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SCB2, histone acetyltransferase |
-Uncharacterized ... , 2 types, 2 molecules CO
| #3: Protein | Mass: 48541.484 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S660 |
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| #14: Protein | Mass: 79972.164 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SD59 |
-Transcription initiation factor TFIID subunit ... , 4 types, 4 molecules DEGI
| #4: Protein | Mass: 83784.141 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SH10 |
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| #5: Protein | Mass: 52463.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S770 |
| #7: Protein | Mass: 21417.871 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0RYR4 |
| #8: Protein | Mass: 83091.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S2A1 |
-Putative transcriptional ... , 2 types, 2 molecules KH
| #9: Protein | Mass: 131755.562 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0S267 |
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| #11: Protein | Mass: 52133.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Thermochaetoides thermophila (fungus) / References: UniProt: G0SED0 |
-Details
| Has protein modification | Y |
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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: Tra1 module of ctSAGA complex / Type: COMPLEX / Entity ID: #10, #2-#6 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Thermochaetoides thermophila (fungus) |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: YES / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| EM embedding | Material: HEPES Buffer |
| Vitrification | Cryogen name: ETHANE |
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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: OTHER |
| Electron lens | Mode: OTHER / Nominal defocus max: 2500 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 68.9 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.5 Å / Resolution method: OTHER / Num. of particles: 3566416 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
| Displacement parameters | Biso mean: 80.37 Å2 | ||||||||||||||||||||||||
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About Yorodumi




Thermochaetoides thermophila (fungus)
United States, 1items
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FIELD EMISSION GUN