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Open data
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Basic information
| Entry | Database: PDB / ID: 9rdk | |||||||||||||||
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| Title | Cryo-EM structure of the human SAGA co-activator complex | |||||||||||||||
Components |
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Keywords | TRANSCRIPTION / Transcription co-activator / Lysine acetyltransferase / complex | |||||||||||||||
| Function / homology | Function and homology informationSAGA-type complex / regulation of somatic stem cell population maintenance / SAGA complex assembly / lateral mesodermal cell differentiation / allantois development / transcription factor TFTC complex / SLIK (SAGA-like) complex / negative regulation of microtubule depolymerization / hepatocyte differentiation / Swr1 complex ...SAGA-type complex / regulation of somatic stem cell population maintenance / SAGA complex assembly / lateral mesodermal cell differentiation / allantois development / transcription factor TFTC complex / SLIK (SAGA-like) complex / negative regulation of microtubule depolymerization / hepatocyte differentiation / Swr1 complex / U12-type spliceosomal complex / RNA splicing, via transesterification reactions / maintenance of protein location in nucleus / splicing factor binding / regulation of double-strand break repair / U2-type precatalytic spliceosome / U2-type prespliceosome assembly / U2-type spliceosomal complex / RNA polymerase binding / SAGA complex / U2 snRNP / transcription preinitiation complex / precatalytic spliceosome / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / transcription factor TFIID complex / RNA polymerase II general transcription initiation factor activity / limb development / nucleus organization / 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 / regulation of RNA splicing / histone deacetylase complex / mRNA Splicing - Minor Pathway / DNA repair-dependent chromatin remodeling / NuA4 histone acetyltransferase complex / positive regulation of transcription initiation by RNA polymerase II / embryonic placenta development / U2 snRNA binding / somitogenesis / regulation of DNA repair / RNA polymerase II preinitiation complex assembly / positive regulation of double-strand break repair via homologous recombination / catalytic step 2 spliceosome / gastrulation / RNA Polymerase II Pre-transcription Events / mRNA Splicing - Major Pathway / visual perception / TBP-class protein binding / RNA splicing / nuclear estrogen receptor binding / male germ cell nucleus / spliceosomal complex / transcription coregulator activity / transcription initiation at RNA polymerase II promoter / DNA-templated transcription initiation / promoter-specific chromatin binding / G1/S transition of mitotic cell cycle / mRNA splicing, via spliceosome / Formation of the beta-catenin:TCF transactivating complex / negative regulation of protein catabolic process / mRNA transcription by RNA polymerase II / microtubule cytoskeleton organization / autophagy / multicellular organism growth / nuclear matrix / cytoplasmic ribonucleoprotein granule / transcription corepressor activity / nucleosome / HATs acetylate histones / microtubule cytoskeleton / positive regulation of cell growth / regulation of apoptotic process / transcription by RNA polymerase II / DNA-binding transcription factor binding / Regulation of TP53 Activity through Phosphorylation / transcription coactivator activity / regulation of cell cycle / Ub-specific processing proteases / nuclear speck / protein stabilization / chromatin remodeling / protein heterodimerization activity / focal adhesion / apoptotic process / regulation of transcription by RNA polymerase II / regulation of DNA-templated transcription / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / protein-containing complex binding / nucleolus / perinuclear region of cytoplasm / enzyme binding / negative regulation of transcription by RNA polymerase II / Golgi apparatus / positive regulation of transcription by RNA polymerase II Similarity search - Function | |||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.41 Å | |||||||||||||||
Authors | Damilot, M. / Ben-Shem, A. / Papai, G. | |||||||||||||||
| Funding support | France, 2items
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Citation | Journal: Sci Adv / Year: 2026Title: Insights into the structure and evolution of the human SAGA complex by affinity-ligand purification. Authors: Mylène Damilot / Thomas Schoeps / Laszlo Tora / Patrick Schultz / Luc Lebeau / Gabor Papai / Adam Ben-Shem / ![]() Abstract: Human SAGA is a 20-subunit transcriptional coactivator. Compared with yeast, metazoan SAGA uniquely incorporates a 150-kDa splicing-factor module (SPL), also present in U2 small nuclear ...Human SAGA is a 20-subunit transcriptional coactivator. Compared with yeast, metazoan SAGA uniquely incorporates a 150-kDa splicing-factor module (SPL), also present in U2 small nuclear ribonucleoprotein (U2snRNP). Metazoan gene duplication further specialized shared TFIID/SAGA subunits into SAGA-specific paralogs (TAF5L and TAF6L), but the functional consequences of this divergence are unknown. We report the structure of endogenous human SAGA purified via an affinity ligand from cells that were not disturbed by any genomic engineering tools. Our work reveals the high-resolution structure of SPL and the TAF6L HEAT repeat domain that provides the SPL with a docking surface. We elucidate how SPL and the HEAT repeats are incorporated into SAGA. We identify major structural differences between TAF6L/TAF5L and their canonical paralogs that enable SPL accommodation. SPL engages SAGA through a substantially smaller interface than in U2snRNP, despite sharing a deeply inserted helical motif. The seemingly weaker interaction of SPL with SAGA raises the possibility that SAGA relays this module to the splicing machinery. | |||||||||||||||
| 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 | 9rdk.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9rdk.ent.gz | 1.1 MB | Display | PDB format |
| PDBx/mmJSON format | 9rdk.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rd/9rdk ftp://data.pdbj.org/pub/pdb/validation_reports/rd/9rdk | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 53937MC C: citing same article ( M: map data used to model this data |
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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
-Transcription ... , 5 types, 5 molecules EGHIM
| #1: Protein | Mass: 27654.861 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: Q9HBM6 |
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| #7: Protein | Mass: 17948.467 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: Q16514 |
| #8: Protein | Mass: 21731.248 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: Q12962 |
| #9: Protein | Mass: 35840.816 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: O75486 |
| #12: Protein | Mass: 85884.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: Q8NEM7 |
-Protein , 6 types, 6 molecules NLCDJK
| #2: Protein | Mass: 95597.742 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: O15265 |
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| #3: Protein | Mass: 66223.047 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: O75529 |
| #5: Protein | Mass: 438139.531 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: Q9Y4A5 |
| #6: Protein | Mass: 46243.629 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: O94864 |
| #10: Protein | Mass: 37432.531 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: Q96BN2 |
| #11: Protein | Mass: 67903.289 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: Q9Y6J9 |
-Splicing factor 3B subunit ... , 2 types, 2 molecules AB
| #4: Protein | Mass: 135718.844 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: Q15393 |
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| #13: Protein | Mass: 10149.369 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K562 / References: UniProt: Q9BWJ5 |
-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: SAGA / Type: COMPLEX / Entity ID: #4, #13, #5-#6, #1, #7-#11, #3, #12, #2 / Source: NATURAL |
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| Molecular weight | Value: 1.6 MDa / Experimental value: YES |
| Source (natural) | Organism: Homo sapiens (human) / Strain: K562 |
| Buffer solution | pH: 8 |
| Specimen | Conc.: 0.15 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| 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: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3500 nm / Nominal defocus min: 1200 nm / Cs: 2.7 mm |
| Specimen holder | Cryogen: NITROGEN / Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||
| Particle selection | Num. of particles selected: 1027610 | ||||||||||||||||||
| 3D reconstruction | Resolution: 2.41 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 272167 / Symmetry type: POINT |
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Homo sapiens (human)
France, 2items
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FIELD EMISSION GUN