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-Structure paper
Title | Assembly of complex viruses exemplified by a halophilic euryarchaeal virus. |
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Journal, issue, pages | Nat Commun, Vol. 10, Issue 1, Page 1456, Year 2019 |
Publish date | Mar 29, 2019 |
![]() | Luigi De Colibus / Elina Roine / Thomas S Walter / Serban L Ilca / Xiangxi Wang / Nan Wang / Alan M Roseman / Dennis Bamford / Juha T Huiskonen / David I Stuart / ![]() ![]() ![]() |
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). ...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. |
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Methods | EM (single particle) |
Resolution | 3.8 - 7.3 Å |
Structure data | EMDB-4633, PDB-6qt9: ![]() EMDB-4634: ![]() EMDB-4656: |
Source |
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![]() | VIRUS / euryarcheal virus / SH1 |