38BO
Arabidopsis H2AXa containing nucleosome, Parallel stack
Summary for 38BO
| Entry DOI | 10.2210/pdb38bo/pdb |
| EMDB information | 78694 |
| Descriptor | Core Histone H2A/H2B/H3 domain-containing protein, Histone H4, Probable histone H2AXa, ... (6 entities in total) |
| Functional Keywords | nucleosome, chromatin, histone, nuclear protein |
| Biological source | Arabidopsis thaliana (thale cress) More |
| Total number of polymer chains | 20 |
| Total formula weight | 426755.93 |
| Authors | |
| Primary citation | Panigrahi, R.,Edwards, R.,Agbagba, N.,Glover, M. Molecular Architecture of the H2AX-Containing Nucleosome from Arabidopsis. Cells, 15:-, 2026 Cited by PubMed Abstract: Nucleosomes integrate diverse histone variants to organize chromatin and coordinate genome maintenance. In plants, the structural interplay between replication-associated histones and DNA damage-responsive histone variants remains poorly understood. Here, we determine cryogenic electron microscopy structures of an () nucleosome containing the replication-associated histones H2B.6 and H3.1 together with the DNA damage-responsive variant H2AXa. The mononucleosome structure, resolved at 2.73 Å, preserves the canonical nucleosome architecture. Unexpectedly, the reconstituted mononucleosomes formed defined higher-order assemblies in the absence of linker DNA or chemical crosslinking. Two distinct nucleosome-nucleosome arrangements, parallel and right offset, were identified. The right offset closely resembles the human counterpart, whereas the parallel arrangement exhibits slight displacement of H2B structural elements at the inter-nucleosomal interface. Together these structures reveal how a distinct histone composition preserves the canonical nucleosome architecture while supporting multiple defined modes of nucleosome packing, providing structural insights into conserved and divergent features of H2AX-containing chromatin organization across plants and animals. PubMed: 42882494DOI: 10.3390/cells15191795 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.75 Å) |
Structure validation
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