7N8N
Melbournevirus nucleosome like particle
Summary for 7N8N
| Entry DOI | 10.2210/pdb7n8n/pdb |
| EMDB information | 24238 |
| Descriptor | Histone H4-H3 doublet, Histone H2B-H2A doublet, DNA (147-MER), ... (4 entities in total) |
| Functional Keywords | nucleosome, virus, dna binding protein, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Melbournevirus More |
| Total number of polymer chains | 6 |
| Total formula weight | 208338.50 |
| Authors | Liu, Y.,Toner, C.M.,Zhou, K.,Bowerman, S.,Luger, K. (deposition date: 2021-06-15, release date: 2021-08-04, Last modification date: 2024-06-05) |
| Primary citation | Liu, Y.,Bisio, H.,Toner, C.M.,Jeudy, S.,Philippe, N.,Zhou, K.,Bowerman, S.,White, A.,Edwards, G.,Abergel, C.,Luger, K. Virus-encoded histone doublets are essential and form nucleosome-like structures. Cell, 184:4237-4250.e19, 2021 Cited by PubMed Abstract: The organization of genomic DNA into defined nucleosomes has long been viewed as a hallmark of eukaryotes. This paradigm has been challenged by the identification of "minimalist" histones in archaea and more recently by the discovery of genes that encode fused remote homologs of the four eukaryotic histones in Marseilleviridae, a subfamily of giant viruses that infect amoebae. We demonstrate that viral doublet histones are essential for viral infectivity, localize to cytoplasmic viral factories after virus infection, and ultimately are found in the mature virions. Cryogenic electron microscopy (cryo-EM) structures of viral nucleosome-like particles show strong similarities to eukaryotic nucleosomes despite the limited sequence identify. The unique connectors that link the histone chains contribute to the observed instability of viral nucleosomes, and some histone tails assume structural roles. Our results further expand the range of "organisms" that require nucleosomes and suggest a specialized function of histones in the biology of these unusual viruses. PubMed: 34297924DOI: 10.1016/j.cell.2021.06.032 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.89 Å) |
Structure validation
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