6H9C

Cryo-EM structure of archaeal extremophilic internal membrane-containing Haloarcula californiae icosahedral virus 1 (HCIV-1) at 3.74 Angstroms resolution.

6H9C の概要

• エントリーDOI: 10.2210/pdb6h9c/pdb
• EMDBエントリー: 0050 0072 0073 0131 0172 0174
• 分子名称: VP7, VP9, GPS-III molecule located underneath the capsomer close to the icosahedral three-fold axis., ... (7 entities in total)
• 機能のキーワード: vertical single beta-barrel virus, internal membrane-containing archaeal virus., virus
• 由来する生物種: Haloarcula californiae ATCC 33799; 詳細
• タンパク質・核酸の鎖数: 32
• 化学式量合計: 648000.32

構造登録者

Abrescia, N.G.,Santos-Perez, I.,Charro, D. (登録日: 2018-08-03, 公開日: 2019-03-27, 最終更新日: 2024-07-10)

主引用文献

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

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: 30862777
DOI: 10.1038/s41467-019-08927-2

実験手法

ELECTRON MICROSCOPY (3.74 Å)