9C4B
Second BAF53a of the human TIP60 complex
Summary for 9C4B
| Entry DOI | 10.2210/pdb9c4b/pdb |
| EMDB information | 45180 |
| Descriptor | Actin-like protein 6A (1 entity in total) |
| Functional Keywords | chromatin modification, gene regulation |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 47509.81 |
| Authors | Yang, Z.,Mameri, A.,Florez Ariza, A.J.,Cote, J.,Nogales, E. (deposition date: 2024-06-03, release date: 2024-08-14, Last modification date: 2024-09-11) |
| Primary citation | Yang, Z.,Mameri, A.,Cattoglio, C.,Lachance, C.,Florez Ariza, A.J.,Luo, J.,Humbert, J.,Sudarshan, D.,Banerjea, A.,Galloy, M.,Fradet-Turcotte, A.,Lambert, J.P.,Ranish, J.A.,Cote, J.,Nogales, E. Structural insights into the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex. Science, 385:eadl5816-eadl5816, 2024 Cited by PubMed Abstract: The human NuA4/TIP60 co-activator complex, a fusion of the yeast SWR1 and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4/H2A/H2A.Z to regulate gene expression and maintain genome stability. Our cryo-electron microscopy studies show that, within the NuA4/TIP60 complex, the EP400 subunit serves as a scaffold holding the different functional modules in specific positions, creating a unique arrangement of the ARP module. EP400 interacts with the TRRAP subunit using a footprint that overlaps with that of the SAGA acetyltransferase complex, preventing the formation of a hybrid complex. Loss of the TRRAP subunit leads to mislocalization of NuA4/TIP60, resulting in the redistribution of H2A.Z and its acetylation across the genome, emphasizing the dual functionality of NuA4/TIP60 as a single macromolecular assembly. PubMed: 39088653DOI: 10.1126/science.adl5816 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
Download full validation report
