6QT9

Cryo-EM structure of SH1 full particle.

Summary for 6QT9

• Entry DOI: 10.2210/pdb6qt9/pdb
• EMDB information: 4633
• Descriptor: ORF 25, ORF 24, ORF 31, ... (8 entities in total)
• Functional Keywords: euryarcheal virus, sh1, virus
• Biological source: Haloarcula hispanica virus SH1; More
• Total number of polymer chains: 30
• Total formula weight: 604188.42

Authors

De Colibus, L.,Roine, E.,Walter, T.S.,Ilca, S.L.,Wang, X.,Wang, N.,Roseman, A.M.,Bamford, D.,Huiskonen, J.T.,Stuart, D.I. (deposition date: 2019-02-22, release date: 2019-04-10, Last modification date: 2024-05-15)

Primary citation

Colibus, L.,Roine, E.,Walter, T.S.,Ilca, S.L.,Wang, X.,Wang, N.,Roseman, A.M.,Bamford, D.,Huiskonen, J.T.,Stuart, D.I.
Assembly of complex viruses exemplified by a halophilic euryarchaeal virus.
Nat Commun, 10:1456-1456, 2019

PubMed Abstract: Many of the largest known viruses belong to the PRD1-adeno structural lineage characterised by conserved pseudo-hexameric capsomers composed of three copies of a single major capsid protein (MCP). Here, by high-resolution cryo-EM analysis, we show that a class of archaeal viruses possess hetero-hexameric MCPs which mimic the PRD1-adeno lineage trimer. These hetero-hexamers are built from heterodimers and utilise a jigsaw-puzzle system of pegs and holes, and underlying minor capsid proteins, to assemble the capsid laterally from the 5-fold vertices. At these vertices proteins engage inwards with the internal membrane vesicle whilst 2-fold symmetric horn-like structures protrude outwards. The horns are assembled from repeated globular domains attached to a central spine, presumably facilitating multimeric attachment to the cell receptor. Such viruses may represent precursors of the main PRD1-adeno lineage, similarly engaging cell-receptors via 5-fold spikes and using minor proteins to define particle size.

PubMed: 30926810
DOI: 10.1038/s41467-019-09451-z

Experimental method

ELECTRON MICROSCOPY (3.8 Å)