+
Open data
-
Basic information
| Entry | ![]() | |||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| Title | Histone Acetyl Transferase (HAT) module of ctSAGA | |||||||||
Map data | ||||||||||
Sample |
| |||||||||
Keywords | ctSAGA complex / Histone Acetyl Transferase (HAT) Module / Tra1 module and Core module / TRANSCRIPTION | |||||||||
| Function / homology | Function and homology informationSAGA-type complex / histone H3 acetyltransferase activity / SAGA complex / histone acetyltransferase complex / histone acetyltransferase / transcription coactivator activity / chromatin remodeling / chromatin binding / regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II ...SAGA-type complex / histone H3 acetyltransferase activity / SAGA complex / histone acetyltransferase complex / histone acetyltransferase / transcription coactivator activity / chromatin remodeling / chromatin binding / regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleus Similarity search - Function | |||||||||
| Biological species | Thermochaetoides thermophila (fungus) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
Authors | Mattoo RUH / Chen DH / Bushnell DA / Tamir S / Kornberg RD | |||||||||
| Funding support | United States, 1 items
| |||||||||
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. | |||||||||
| History |
|
-
Structure visualization
| Supplemental images |
|---|
-
Downloads & links
-EMDB archive
| Map data | emd_73235.map.gz | 59.7 MB | EMDB map data format | |
|---|---|---|---|---|
| Header (meta data) | emd-73235-v30.xml emd-73235.xml | 18.6 KB 18.6 KB | Display Display | EMDB header |
| Images | emd_73235.png | 43.5 KB | ||
| Filedesc metadata | emd-73235.cif.gz | 6.6 KB | ||
| Others | emd_73235_half_map_1.map.gz emd_73235_half_map_2.map.gz | 49.7 MB 49.6 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-73235 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-73235 | HTTPS FTP |
-Validation report
| Summary document | emd_73235_validation.pdf.gz | 776.6 KB | Display | EMDB validaton report |
|---|---|---|---|---|
| Full document | emd_73235_full_validation.pdf.gz | 776.2 KB | Display | |
| Data in XML | emd_73235_validation.xml.gz | 11.9 KB | Display | |
| Data in CIF | emd_73235_validation.cif.gz | 13.9 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-73235 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-73235 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9ynvMC ![]() 9ynuC ![]() 9ynwC ![]() 9yolC ![]() 9yoqC ![]() 9yzyC M: atomic model generated by this map C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
|---|---|
| Related items in Molecule of the Month |
-
Map
| File | Download / File: emd_73235.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.041 Å | ||||||||||||||||||||||||||||||||||||
| Density |
| ||||||||||||||||||||||||||||||||||||
| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
|
-Supplemental data
-Half map: #2
| File | emd_73235_half_map_1.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-Half map: #1
| File | emd_73235_half_map_2.map | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Projections & Slices |
| ||||||||||||
| Density Histograms |
-
Sample components
-Entire : Minimal HAT module of ctSAGA complex
| Entire | Name: Minimal HAT module of ctSAGA complex |
|---|---|
| Components |
|
-Supramolecule #1: Minimal HAT module of ctSAGA complex
| Supramolecule | Name: Minimal HAT module of ctSAGA complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
|---|---|
| Source (natural) | Organism: Thermochaetoides thermophila (fungus) |
-Macromolecule #1: Putative transcriptional coactivator HFI1 protein
| Macromolecule | Name: Putative transcriptional coactivator HFI1 protein / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
|---|---|
| Source (natural) | Organism: Thermochaetoides thermophila (fungus) |
| Molecular weight | Theoretical: 52.133355 KDa |
| Sequence | String: MVDINPAALS RPSIGLSTPS FPGKSGSINV SVPSSASASA SASSAHSKPQ KTSLVPPRID LEPIYTALKA AIGAEQWPVY KETLTNFLI GRLNQAELSE RIDPILASQD GQKEHLHNQL IAAIYANVTR EMPDPGLAPW VSANDKPTTA QTKPVTGDAN E RRLKGEVM ...String: MVDINPAALS RPSIGLSTPS FPGKSGSINV SVPSSASASA SASSAHSKPQ KTSLVPPRID LEPIYTALKA AIGAEQWPVY KETLTNFLI GRLNQAELSE RIDPILASQD GQKEHLHNQL IAAIYANVTR EMPDPGLAPW VSANDKPTTA QTKPVTGDAN E RRLKGEVM QLPARDRRRI KELAHNDFDP YDALANVLME HARAKPPKIA EPPASAGGLK MNFDLEIRKR YAQPLAVESG EF PDTSNIE SRMLPFCYEA GLSSGHAPDA AQFMSIATET FIKEVMSAIF SRTRSNGPGD SGSAGFGLGS GWIQTHRYRK QLA KEEEAF QRGEISRDKM GLLPVEAKAA SERGPLGMAD VRLALEMGDC GLAGFPVIVK SVIYGWREGE LENWEDYTYV DPSR PDGIA IPSRGDGDVE MGGVGVNGVV KGEPEPQQQP LANGVHDVDA MDIDGVSVAG GAANEIWWEG AEPETSDLLN AVLDS CLAV N UniProtKB: Putative transcriptional coactivator HFI1 protein |
-Macromolecule #2: histone acetyltransferase
| Macromolecule | Name: histone acetyltransferase / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: histone acetyltransferase |
|---|---|
| Source (natural) | Organism: Thermochaetoides thermophila (fungus) |
| Molecular weight | Theoretical: 46.983691 KDa |
| Sequence | String: MTSENGKRKA TEEPGSPSAA KRIKQEPSET DKDKKEENKD KKTVAKPPPI PYPEKPAVIE ERNGEIEFRV VNNDGERESL IILTGLKCI FQKQLPKMPK DYIARLVYDR THLSIAIVKK PLEVVGGITY RPFKNRKFAE IVFCAISSDQ QVKGYGAHLM S HLKDYVKA ...String: MTSENGKRKA TEEPGSPSAA KRIKQEPSET DKDKKEENKD KKTVAKPPPI PYPEKPAVIE ERNGEIEFRV VNNDGERESL IILTGLKCI FQKQLPKMPK DYIARLVYDR THLSIAIVKK PLEVVGGITY RPFKNRKFAE IVFCAISSDQ QVKGYGAHLM S HLKDYVKA TTNIEHFLTY ADNYAIGYFK KQGFTKEITL DKSVWMGYIK DYEGGTIMQC TMIPRIRYLE QGRMLLKQKE CV QAKIRAF SKSHIVHPPP KQWRNGNVTP IDPLSIDAIR ESGWSPDMDE LARQPRHGPN YNQLLHLLND MQNHASSWPF LVP VNKDEV VDYYDIIKEP MDLSTMESKL EADQYQTPED FIRDAKLIFD NCRKYNNENT PYAKSANKLE KFMWQQIRQI PEWS HLEPS UniProtKB: histone acetyltransferase |
-Macromolecule #3: Transcriptional adapter 2
| Macromolecule | Name: Transcriptional adapter 2 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
|---|---|
| Source (natural) | Organism: Thermochaetoides thermophila (fungus) |
| Molecular weight | Theoretical: 58.86607 KDa |
| Sequence | String: MGVIRKKIAG RSGEGGVKYI CDVCSVDITS TVRIRCADPA CHDYDLCVPC FANGSSSNAH KPATHSFRVI EQNSFPIFDP DWGADEELL LLEGAEIYGL GSWADIADHI GGYRTKDEVR DHYLKVYIES PNFPLPERCS PYDLELPNSI SREEFQARKK R RIEERREA ...String: MGVIRKKIAG RSGEGGVKYI CDVCSVDITS TVRIRCADPA CHDYDLCVPC FANGSSSNAH KPATHSFRVI EQNSFPIFDP DWGADEELL LLEGAEIYGL GSWADIADHI GGYRTKDEVR DHYLKVYIES PNFPLPERCS PYDLELPNSI SREEFQARKK R RIEERREA AKNAPPPQPK TKPTASIPAC HEIQGYMPGR LEFETEYCNE AEEAVQLMSF DPGDGINPRT GELEPEMELK LT VMEIYNN RLTQRVERKK VIFEHNLLEY RENTKAEKKR SREERELLNK AKPFARMMNR HDFEQFCQGL IDELNLRQAI AQL QEWRSM RIGDLKSGEK YEQEKALRIQ KSMPMGSLDR ERLATSQRGK NQQQPEPPSG AALLVAPELP ARYKEPIIDA NGFP RPDAN RLTVDGGSVV VANGTSQPKP KYVPPPVPGV QPMNLTQDNA PDLHLLTPEE IKLCETLRIQ PKPYIMIKEQ ILKEA VKGN GSLKKKQAKE ICRLDSQKGG RIFDFMVNAG WVVKA UniProtKB: Transcriptional adapter 2 |
-Macromolecule #4: Uncharacterized protein
| Macromolecule | Name: Uncharacterized protein / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
|---|---|
| Source (natural) | Organism: Thermochaetoides thermophila (fungus) |
| Molecular weight | Theoretical: 79.972164 KDa |
| Sequence | String: MAPSSSQKGT GKKAGSAASA IRSHQQHSQQ QRSRNTTPGP AGIPPTSSTS VSVSVASLPP IETVETETLD LRFDTFRNVT FEDLVDPAA ASALIPDSKS LDGIISRLQR LADIIEKRGA NCDRGMRLLA QTRRQRLDEL AVERGREEER RQAEADDEKK A NKKKRKAD ...String: MAPSSSQKGT GKKAGSAASA IRSHQQHSQQ QRSRNTTPGP AGIPPTSSTS VSVSVASLPP IETVETETLD LRFDTFRNVT FEDLVDPAA ASALIPDSKS LDGIISRLQR LADIIEKRGA NCDRGMRLLA QTRRQRLDEL AVERGREEER RQAEADDEKK A NKKKRKAD SLAPGAVNTE RSSPNRESTS KARKLDRDDT ASSSLSPAAA GTPSNMDVDD KDKEKDKDKT KAEADSDSDS DD GAPPPPP RPPANVFGDD PSTFPDPTVY EIRPVLPGMS EEEIKEIYSV ASYPKSDLAH LTCGEPPDRD FSNSKPTNQI NFS TFSSYI EPYFRPFTEE DLAFLRERGD RVTPFIMPKR GKKHYTEIWA EEDGAMAIDS SPPGGRDRLP PNQARGSIDN MDDE VAETD KLSVGPLLTR LLQAMRPENR APTADDKSGP NGTSGDGDGP QQSFDFNDST AAPNPSQSQP NGVNGVAATT NGDSQ QQQQ QQQHQSLPPA TFMPESNTEA WKKATHPKLD YNQVDERIKQ ELRHIGFLPL PPSSATDPSN SSASVTPAAP PPPGTT ATT AEYDGHYDDE VAARLRVLQA RLREQILLNG ARKARLTELV KERMAYQEYQ TILEDLDAQV NAAYLKRTRT MGKKPKK NR PGQHSSGSAA AAAAAAAGMA RPGIGDLART LMDRRRRWIE QIGAVFDDEG ITKCPRVEDG DTSIFGREIM AELIKREK E AWDEEVEEE UniProtKB: Uncharacterized protein |
-Experimental details
-Structure determination
| Method | cryo EM |
|---|---|
Processing | single particle reconstruction |
| Aggregation state | particle |
-
Sample preparation
| Buffer | pH: 7.5 |
|---|---|
| Sugar embedding | Material: HEPES Buffer |
| Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
| Microscope | TFS KRIOS |
|---|---|
| Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 68.9 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
Movie
Controller
About Yorodumi




Keywords
Thermochaetoides thermophila (fungus)
Authors
United States, 1 items
Citation






















Z (Sec.)
Y (Row.)
X (Col.)




































Processing
FIELD EMISSION GUN
