7ATA
Nudaurelia capensis omega virus procapsid: virus-like particles expressed in Nicotiana benthamiana
これはPDB形式変換不可エントリーです。
7ATA の概要
| エントリーDOI | 10.2210/pdb7ata/pdb |
| 関連するPDBエントリー | 7ANM |
| EMDBエントリー | 11911 |
| 分子名称 | p70 (2 entities in total) |
| 機能のキーワード | icosahedral virus, auto-catalytic cleavage, virus maturation, transient expression, virus like particle |
| 由来する生物種 | Nudaurelia capensis omega virus 詳細 |
| タンパク質・核酸の鎖数 | 8 |
| 化学式量合計 | 279639.72 |
| 構造登録者 | Castells-Graells, R.,Ribeiro, J.R.S.,Domitrovic, T.,Hesketh, E.L.,Scarff, C.A.,Johnson, J.E.,Ranson, N.A.,Lawson, D.M.,Lomonossoff, G.P. (登録日: 2020-10-29, 公開日: 2021-08-25, 最終更新日: 2024-11-06) |
| 主引用文献 | Castells-Graells, R.,Ribeiro, J.R.S.,Domitrovic, T.,Hesketh, E.L.,Scarff, C.A.,Johnson, J.E.,Ranson, N.A.,Lawson, D.M.,Lomonossoff, G.P. Plant-expressed virus-like particles reveal the intricate maturation process of a eukaryotic virus. Commun Biol, 4:619-619, 2021 Cited by PubMed Abstract: Many virus capsids undergo exquisitely choreographed maturation processes in their host cells to produce infectious virions, and these remain poorly understood. As a tool for studying virus maturation, we transiently expressed the capsid protein of the insect virus Nudaurelia capensis omega virus (NωV) in Nicotiana benthamiana and were able to purify both immature procapsids and mature capsids from infiltrated leaves by varying the expression time. Cryo-EM analysis of the plant-produced procapsids and mature capsids to 6.6 Å and 2.7 Å resolution, respectively, reveals that in addition to large scale rigid body motions, internal regions of the subunits are extensively remodelled during maturation, creating the active site required for autocatalytic cleavage and infectivity. The mature particles are biologically active in terms of their ability to lyse membranes and have a structure that is essentially identical to authentic virus. The ability to faithfully recapitulate and visualize a complex maturation process in plants, including the autocatalytic cleavage of the capsid protein, has revealed a ~30 Å translation-rotation of the subunits during maturation as well as conformational rearrangements in the N and C-terminal helical regions of each subunit. PubMed: 34031522DOI: 10.1038/s42003-021-02134-w 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (6.63 Å) |
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