9NH8
CHD1-nucleosome complex (anchored state)
Summary for 9NH8
| Entry DOI | 10.2210/pdb9nh8/pdb |
| EMDB information | 42693 49406 |
| Descriptor | Histone H3.2, Histone H4, Histone H2A, ... (8 entities in total) |
| Functional Keywords | chromatin, remodeler, genome organization, nuclear protein, nuclear protein-dna complex, nuclear protein/dna |
| Biological source | Xenopus laevis (African clawed frog) More |
| Total number of polymer chains | 12 |
| Total formula weight | 403252.77 |
| Authors | James, A.M.,Farnung, L. (deposition date: 2025-02-24, release date: 2025-05-07, Last modification date: 2025-05-21) |
| Primary citation | James, A.M.,Farnung, L. Structural basis of human CHD1 nucleosome recruitment and pausing. Mol.Cell, 2025 Cited by PubMed Abstract: Chromatin remodelers regulate gene expression and genome maintenance by controlling nucleosome positioning, but the structural basis for their regulated and directional activity remains poorly understood. Here, we present three cryoelectron microscopy (cryo-EM) structures of human chromodomain helicase DNA-binding protein 1 (CHD1) bound to nucleosomes that reveal previously unobserved recruitment and regulatory states. We identify a structural element, termed the "anchor element," that connects the CHD1 ATPase motor to the nucleosome entry-side acidic patch. The anchor element coordinates with other regulatory modules, including the gating element, which undergoes a conformational switch critical for remodeling. Our structures demonstrate how the DNA-binding region of CHD1 binds entry- and exit-side DNA during remodeling to achieve directional sliding. The observed structural elements are conserved across chromatin remodelers, suggesting a unified mechanism for nucleosome recognition and remodeling. Our findings show how chromatin remodelers couple nucleosome recruitment to regulated DNA translocation, providing a framework for understanding chromatin remodeler mechanisms beyond DNA translocation. PubMed: 40334658DOI: 10.1016/j.molcel.2025.04.020 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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