9JC6
Human H2BW2 nucleosome
Summary for 9JC6
| Entry DOI | 10.2210/pdb9jc6/pdb |
| EMDB information | 61358 |
| Descriptor | Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (6 entities in total) |
| Functional Keywords | nucleosome, dna binding protein, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 10 |
| Total formula weight | 204747.08 |
| Authors | Ding, D.B.,Ishibashi, T.,Nguyen, T.T. (deposition date: 2024-08-28, release date: 2025-09-03, Last modification date: 2025-09-24) |
| Primary citation | Nguyen, A.T.T.,Ding, D.,Bai, X.,Pang, M.Y.H.,Deng, M.,Liu, Y.,Jin, T.,Xu, Z.,Zhang, Y.,Zhai, Y.,Yan, Y.,Ishibashi, T. H2B.W2, a spermatocyte-specific histone variant, disrupts nucleosome stability, and reduces chromatin compaction. Nucleic Acids Res., 53:-, 2025 Cited by PubMed Abstract: Spermatogenesis is a highly regulated process that requires precise chromatin remodeling, which includes the incorporation of testis-specific histone variants. While several of these variants have been characterized, the role of H2B.W2, a member of the H2BW family, remains largely unclear. Here, we showed that H2B.W2 expression occurs mainly in spermatocytes, slightly later than its paralog H2B.W1. Cryo-electron microscopy analysis of H2B.W2-containing nucleosomes reveals a more relaxed conformation compared to canonical nucleosomes caused by weakened interactions between the outer DNA turn and the histone core. We pinpointed the N-terminal tail and α2 helix of H2B.W2 as critical regions for nucleosome destabilization. Furthermore, we identify G73 within the L1 loop as a key residue involved in disrupting higher-order chromatin structure. Our findings suggest that H2B.W2-mediated nucleosome and chromatin destabilization may play a role in regulating gene expression during spermatogenesis, with potential implications for sperm development and function. PubMed: 40874595DOI: 10.1093/nar/gkaf825 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.34 Å) |
Structure validation
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