9CVT
Melbournevirus Mini variant Nucleosome
Summary for 9CVT
| Entry DOI | 10.2210/pdb9cvt/pdb |
| Related | 7n8n |
| EMDB information | 45966 |
| Descriptor | Histone doublet miniH2B-H2A, Histone doublet H4-H3, Widom 601 Strand 1, ... (4 entities in total) |
| Functional Keywords | histone, nucleosome, virus, viral protein, viral protein-dna complex, viral protein/dna |
| Biological source | Melbournevirus More |
| Total number of polymer chains | 6 |
| Total formula weight | 176213.84 |
| Authors | Villalta, A.,Luger, K. (deposition date: 2024-07-29, release date: 2025-07-30, Last modification date: 2025-09-03) |
| Primary citation | Villalta, A.,Bisio, H.,Toner, C.M.,Abergel, C.,Luger, K. Melbournevirus encodes a shorter H2B-H2A doublet histone variant that forms structurally distinct nucleosome structures. Nat Commun, 16:6903-6903, 2025 Cited by PubMed Abstract: Unique among viruses, some giant viruses utilize histones to organize their genomes into nucleosomes. Melbournevirus encodes a distinct H2B-H2A histone doublet variant in addition to the canonical H4-H3 and H2B-H2A doublets. This viral histone variant has a truncated H2B portion and its amino acid sequence deviates from that of the main viral H2B-H2A throughout the entire coding region. It is less abundant than the main H2B-H2A doublet, is likely essential for melbournevirus fitness, and is conserved in all Marseilleviridae. The cryo-EM structure of a nucleosome-like particle reconstituted with this H2B-H2A variant and viral H4-H3 reveals that only 90 base pairs of DNA are stably bound, significantly less than in eukaryotic nucleosomes and viral nucleosomes made with the main fused viral histone doublets. The reduced ability to bind DNA can be attributed to structural differences between variant and main H2B-H2A. Variant melbournevirus nucleosomes are less stable, possibly aiding rapid genome unpacking to initiate gene expression. Our results highlight the remarkable propensity of giant viruses to appropriate the utility of histones for their specialized purposes. PubMed: 40715086DOI: 10.1038/s41467-025-62031-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.41 Å) |
Structure validation
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