7KTS
Negative stain EM structure of the human SAGA coactivator complex (TRRAP, core, splicing module)
This is a non-PDB format compatible entry.
Summary for 7KTS
| Entry DOI | 10.2210/pdb7kts/pdb |
| EMDB information | 23027 23028 |
| Descriptor | Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein, Transcriptional adapter 1, Ataxin-7, ... (13 entities in total) |
| Functional Keywords | splicing, gene regulation, transcription, chromatin |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 13 |
| Total formula weight | 1100242.14 |
| Authors | Herbst, D.A.,Esbin, M.N.,Nogales, E. (deposition date: 2020-11-24, release date: 2021-11-10, Last modification date: 2024-05-29) |
| Primary citation | Herbst, D.A.,Esbin, M.N.,Louder, R.K.,Dugast-Darzacq, C.,Dailey, G.M.,Fang, Q.,Darzacq, X.,Tjian, R.,Nogales, E. Structure of the human SAGA coactivator complex. Nat.Struct.Mol.Biol., 28:989-996, 2021 Cited by PubMed Abstract: The SAGA complex is a regulatory hub involved in gene regulation, chromatin modification, DNA damage repair and signaling. While structures of yeast SAGA (ySAGA) have been reported, there are noteworthy functional and compositional differences for this complex in metazoans. Here we present the cryogenic-electron microscopy (cryo-EM) structure of human SAGA (hSAGA) and show how the arrangement of distinct structural elements results in a globally divergent organization from that of yeast, with a different interface tethering the core module to the TRRAP subunit, resulting in a dramatically altered geometry of functional elements and with the integration of a metazoan-specific splicing module. Our hSAGA structure reveals the presence of an inositol hexakisphosphate (InsP) binding site in TRRAP and an unusual property of its pseudo-(Ψ)PIKK. Finally, we map human disease mutations, thus providing the needed framework for structure-guided drug design of this important therapeutic target for human developmental diseases and cancer. PubMed: 34811519DOI: 10.1038/s41594-021-00682-7 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (19.09 Å) |
Structure validation
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