6QCC

Cryo-EM Atomic Structure of Broad Bean Stain Virus (BBSV)

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6QCC の概要

• エントリーDOI: 10.2210/pdb6qcc/pdb
• EMDBエントリー: 4504
• 分子名称: Large coat-protein subunit, Small coat-protein subunit (2 entities in total)
• 機能のキーワード: comovirus capsid plant virus bbsv, virus
• 由来する生物種: Broad bean stain virus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64837.64

構造登録者

Lecorre, F.,Lai Jee Him, J.,Blanc, S.,Zeddam, J.-L.,Trapani, S.,Bron, P. (登録日: 2018-12-27, 公開日: 2019-05-01, 最終更新日: 2024-05-15)

主引用文献

Lecorre, F.,Lai-Kee-Him, J.,Blanc, S.,Zeddam, J.L.,Trapani, S.,Bron, P.
The cryo-electron microscopy structure of Broad Bean Stain Virus suggests a common capsid assembly mechanism among comoviruses.
Virology, 530:75-84, 2019

PubMed Abstract: The Broad bean stain virus (BBSV) is a member of the genus Comovirus infecting Fabaceae. The virus is transmitted through seed and by plant weevils causing severe and widespread disease worldwide. BBSV has a bipartite, positive-sense, single-stranded RNA genome encapsidated in icosahedral particles. We present here the cryo-electron microscopy reconstruction of the BBSV and an atomic model of the capsid proteins refined at 3.22 Å resolution. We identified residues involved in RNA/capsid interactions revealing a unique RNA genome organization. Inspection of the small coat protein C-terminal domain highlights a maturation cleavage between Leu567 and Leu568 and interactions of the C-terminal stretch with neighbouring small coat proteins within the capsid pentameric turrets. These interactions previously proposed to play a key role in the assembly of the Cowpea mosaic virus suggest a common capsid assembly mechanism throughout all comovirus species.

PubMed: 30782565
DOI: 10.1016/j.virol.2019.02.009

実験手法

ELECTRON MICROSCOPY (3.22 Å)