9Y3D
Extended cryo-EM structure of the human SRCAP-nucleosome complex in the fully-engaged state, with H4-bound GAS41
This is a non-PDB format compatible entry.
Summary for 9Y3D
| Entry DOI | 10.2210/pdb9y3d/pdb |
| EMDB information | 71627 |
| Descriptor | Helicase SRCAP, YEATS domain-containing protein 4, Histone H2A type 1, ... (20 entities in total) |
| Functional Keywords | chromatin remodeler, snf2 family atpase, h2a.z, gene regulation, hydrolase-dna binding protein-dna complex, hydrolase/dna binding protein/dna |
| Biological source | Xenopus laevis (African clawed frog) More |
| Total number of polymer chains | 25 |
| Total formula weight | 1258088.23 |
| Authors | |
| Primary citation | Park, G.,Wu, C.,Louder, R.K. Structural mechanism of histone H2A.Z exchange by human SRCAP-CFDP1 holoenzyme. Sci Adv, 12:eaei7728-eaei7728, 2026 Cited by PubMed Abstract: The conserved yeast SWR1 and human SRCAP chromatin remodeling complexes catalyze exchange of nucleosomal histone H2A for H2A.Z, but the underlying mechanism has remained obscure. Here, we show that histone exchange by SRCAP requires the transient activator CFDP1 and resolve nine cryo-electron microscopy structures of the SRCAP-CFDP1 holoenzyme that define the stepwise exchange mechanism. CFDP1 recognizes the conformation of the fully engaged SRCAP-nucleosome complex through interactions with multiple subunits-including direct contact with the ATPase domain-and induces conformational transitions that drive extensive DNA unwrapping, eviction of the H2A-H2B dimer, and insertion of the H2A.Z-H2B dimer, all without necessarily requiring hydrolysis of bound ATP. Collectively, these findings provide unprecedented insight into the mechanism of activator- and nucleotide-driven histone exchange from nucleosomal H2A to H2A.Z. PubMed: 42536744DOI: 10.1126/sciadv.aei7728 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.1 Å) |
Structure validation
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