6TBM
Structure of SAGA bound to TBP, including Spt8 and DUB
Summary for 6TBM
| Entry DOI | 10.2210/pdb6tbm/pdb |
| Related | 6TB4 |
| EMDB information | 10438 10440 10441 10446 |
| Descriptor | TATA-box Binding Protein (TBP), Subunit (60 kDa) of TFIID and SAGA complexes, Subunit (17 kDa) of TFIID and SAGA complexes, involved in RNA polymerase II transcription initiation, ... (19 entities in total) |
| Functional Keywords | transcriptional co-activator, histone-acetylation, transcription |
| Biological source | Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) More |
| Total number of polymer chains | 18 |
| Total formula weight | 1280340.27 |
| Authors | Papai, G.,Frechard, A.,Kolesnikova, O.,Crucifix, C.,Schultz, P.,Ben-Shem, A. (deposition date: 2019-11-01, release date: 2020-02-12, Last modification date: 2024-09-25) |
| Primary citation | Papai, G.,Frechard, A.,Kolesnikova, O.,Crucifix, C.,Schultz, P.,Ben-Shem, A. Structure of SAGA and mechanism of TBP deposition on gene promoters. Nature, 577:711-716, 2020 Cited by PubMed Abstract: SAGA (Spt-Ada-Gcn5-acetyltransferase) is a 19-subunit complex that stimulates transcription via two chromatin-modifying enzymatic modules and by delivering the TATA box binding protein (TBP) to nucleate the pre-initiation complex on DNA, a pivotal event in the expression of protein-encoding genes. Here we present the structure of yeast SAGA with bound TBP. The core of the complex is resolved at 3.5 Å resolution (0.143 Fourier shell correlation). The structure reveals the intricate network of interactions that coordinate the different functional domains of SAGA and resolves an octamer of histone-fold domains at the core of SAGA. This deformed octamer deviates considerably from the symmetrical analogue in the nucleosome and is precisely tuned to establish a peripheral site for TBP, where steric hindrance represses binding of spurious DNA. Complementary biochemical analysis points to a mechanism for TBP delivery and release from SAGA that requires transcription factor IIA and whose efficiency correlates with the affinity of DNA to TBP. We provide the foundations for understanding the specific delivery of TBP to gene promoters and the multiple roles of SAGA in regulating gene expression. PubMed: 31969704DOI: 10.1038/s41586-020-1944-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (20 Å) |
Structure validation
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