6tbm

Structure of SAGA bound to TBP, including Spt8 and DUBStructure of SAGA bound to TBP, including Spt8 and DUB

6tbm, resolution 20.00Å Show:Asymmetric Unit Biological Assembly Structural highlights 6tbm is a 10 chain structure with sequence from Komagataella phaffii GS115. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 20Å Ligands: Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TBP_YEAST General transcription factor that functions at the core of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. Publication Abstract from PubMed 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(1). Here we present the structure of yeast SAGA with bound TBP. The core of the complex is resolved at 3.5 A 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. Structure of SAGA and mechanism of TBP deposition on gene promoters.,Papai G, Frechard A, Kolesnikova O, Crucifix C, Schultz P, Ben-Shem A Nature. 2020 Jan;577(7792):711-716. doi: 10.1038/s41586-020-1944-2. Epub 2020 Jan, 22. PMID:31969704 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also SAGA-associated factor TATA-binding protein 3D structures Transcription initiation factors 3D structures