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-Structure paper
タイトル | Structural basis for assembly of vertical single β-barrel viruses. |
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ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 1184, Year 2019 |
掲載日 | 2019年3月12日 |
![]() | Isaac Santos-Pérez / Diego Charro / David Gil-Carton / Mikel Azkargorta / Felix Elortza / Dennis H Bamford / Hanna M Oksanen / Nicola G A Abrescia / ![]() ![]() |
PubMed 要旨 | 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. |
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手法 | EM (単粒子) |
解像度 | 3.74 - 18.2 Å |
構造データ | ![]() EMDB-0050: ![]() EMDB-0072: ![]() EMDB-0073: ![]() EMDB-0131: |
由来 |
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![]() | VIRUS / single vertical beta-barrel virus / archaeal / membrane-containing / quasi-atomic resolution / vertical single beta-barrel virus / internal membrane-containing archaeal virus. |