6H9C
Cryo-EM structure of archaeal extremophilic internal membrane-containing Haloarcula californiae icosahedral virus 1 (HCIV-1) at 3.74 Angstroms resolution.
Summary for 6H9C
Entry DOI | 10.2210/pdb6h9c/pdb |
EMDB information | 0050 0072 0073 0131 0172 0174 |
Descriptor | VP7, VP9, GPS-III molecule located underneath the capsomer close to the icosahedral three-fold axis., ... (7 entities in total) |
Functional Keywords | vertical single beta-barrel virus, internal membrane-containing archaeal virus., virus |
Biological source | Haloarcula californiae ATCC 33799 More |
Total number of polymer chains | 32 |
Total formula weight | 648000.32 |
Authors | Abrescia, N.G.,Santos-Perez, I.,Charro, D. (deposition date: 2018-08-03, release date: 2019-03-27, Last modification date: 2024-07-10) |
Primary citation | Santos-Perez, I.,Charro, D.,Gil-Carton, D.,Azkargorta, M.,Elortza, F.,Bamford, D.H.,Oksanen, H.M.,Abrescia, N.G.A. Structural basis for assembly of vertical single beta-barrel viruses. Nat Commun, 10:1184-1184, 2019 Cited by PubMed Abstract: The vertical double β-barrel major capsid protein (MCP) fold, fingerprint of the PRD1-adeno viral lineage, is widespread in many viruses infecting organisms across the three domains of life. The discovery of PRD1-like viruses with two MCPs challenged the known assembly principles. Here, we present the cryo-electron microscopy (cryo-EM) structures of the archaeal, halophilic, internal membrane-containing Haloarcula californiae icosahedral virus 1 (HCIV-1) and Haloarcula hispanica icosahedral virus 2 (HHIV-2) at 3.7 and 3.8 Å resolution, respectively. Our structures reveal proteins located beneath the morphologically distinct two- and three-tower capsomers and homopentameric membrane proteins at the vertices that orchestrate the positioning of pre-formed vertical single β-barrel MCP heterodimers. The cryo-EM based structures together with the proteomics data provide insights into the assembly mechanism of this type of viruses and into those with membrane-less double β-barrel MCPs. PubMed: 30862777DOI: 10.1038/s41467-019-08927-2 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.74 Å) |
Structure validation
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