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Title | Structural basis for assembly of vertical single β-barrel viruses. |
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Journal, issue, pages | Nat Commun, Vol. 10, Issue 1, Page 1184, Year 2019 |
Publish date | Mar 12, 2019 |
Authors | Isaac Santos-Pérez / Diego Charro / David Gil-Carton / Mikel Azkargorta / Felix Elortza / Dennis H Bamford / Hanna M Oksanen / Nicola G A Abrescia / |
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 ...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. |
External links | Nat Commun / PubMed:30862777 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.74 - 18.2 Å |
Structure data | EMDB-0050: EMDB-0072: EMDB-0073: EMDB-0131: |
Source |
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Keywords | VIRUS / single vertical beta-barrel virus / archaeal / membrane-containing / quasi-atomic resolution / vertical single beta-barrel virus / internal membrane-containing archaeal virus. |