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8RBS

Emiliania huxleyi virus 201 (EhV-201) asymmetrical unit of capsid proteins predicted by AlphaFold2 fitted into the cryo-EM density of EhV-201 virion composite map.

This is a non-PDB format compatible entry.
Replaces:  8PFN
Summary for 8RBS
Entry DOI10.2210/pdb8rbs/pdb
EMDB information19035
DescriptorMajor capsid protein, Penton protein (2 entities in total)
Functional Keywordscryo-em, subtomogram averaging, ehv-201, enveloped virus, capsid, major capsid protein, composite map, virus
Biological sourceEmiliania huxleyi virus 201
More
Total number of polymer chains85
Total formula weight4705085.95
Authors
Homola, M.,Buttner, C.R.,Fuzik, T.,Novacek, J.,Chaillet, M.,Forster, F.,Plevka, P. (deposition date: 2023-12-04, release date: 2023-12-20, Last modification date: 2024-04-24)
Primary citationHomola, M.,Buttner, C.R.,Fuzik, T.,Krepelka, P.,Holbova, R.,Novacek, J.,Chaillet, M.L.,Zak, J.,Grybchuk, D.,Forster, F.,Wilson, W.H.,Schroeder, D.C.,Plevka, P.
Structure and replication cycle of a virus infecting climate-modulating alga Emiliania huxleyi.
Sci Adv, 10:eadk1954-eadk1954, 2024
Cited by
PubMed Abstract: The globally distributed marine alga has cooling effect on the Earth's climate. The population density of is restricted by viruses, including virus 201 (EhV-201). Despite the impact of viruses on the climate, there is limited information about their structure and replication. Here, we show that the dsDNA genome inside the EhV-201 virion is protected by an inner membrane, capsid, and outer membrane. EhV-201 virions infect by using fivefold vertices to bind to and fuse the virus' inner membrane with the cell plasma membrane. Progeny virions assemble in the cytoplasm at the surface of endoplasmic reticulum-derived membrane segments. Genome packaging initiates synchronously with the capsid assembly and completes through an aperture in the forming capsid. The genome-filled capsids acquire an outer membrane by budding into intracellular vesicles. EhV-201 infection induces a loss of surface protective layers from cells, which enables the continuous release of virions by exocytosis.
PubMed: 38598627
DOI: 10.1126/sciadv.adk1954
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (18 Å)
Structure validation

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