5A32

Electron cryo-microscopy of Cowpea Mosaic Virus containing RNA-1 (CPMVb)

5A32 の概要

• エントリーDOI: 10.2210/pdb5a32/pdb
• 関連するPDBエントリー: 5A33
• EMDBエントリー: 3013
• 分子名称: RNA2 POLYPROTEIN (2 entities in total)
• 機能のキーワード: virus, cpmv, comoviridae, picornavirales.
• 由来する生物種: COWPEA MOSAIC VIRUS (CPMV); 詳細
• 細胞内の位置: Movement protein: Host cell junction, host plasmodesma. Large coat protein: Virion : P03599 P03599
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 61820.00

構造登録者

Hesketh, E.L.,Meshcheriakova, Y.,Dent, K.C.,Saxena, P.,Thompson, R.,Cockburn, J.J.,Lomonossoff, G.P.,Ranson, N.A. (登録日: 2015-05-27, 公開日: 2015-12-23, 最終更新日: 2024-05-08)

主引用文献

Hesketh, E.L.,Meshcheriakova, Y.,Dent, K.C.,Saxena, P.,Thompson, R.F.,Cockburn, J.J.,Lomonossoff, G.P.,Ranson, N.A.
Mechanisms of assembly and genome packaging in an RNA virus revealed by high-resolution cryo-EM.
Nat Commun, 6:10113-10113, 2015

PubMed Abstract: Cowpea mosaic virus is a plant-infecting member of the Picornavirales and is of major interest in the development of biotechnology applications. Despite the availability of >100 crystal structures of Picornavirales capsids, relatively little is known about the mechanisms of capsid assembly and genome encapsidation. Here we have determined cryo-electron microscopy reconstructions for the wild-type virus and an empty virus-like particle, to 3.4 Å and 3.0 Å resolution, respectively, and built de novo atomic models of their capsids. These new structures reveal the C-terminal region of the small coat protein subunit, which is essential for virus assembly and which was missing from previously determined crystal structures, as well as residues that bind to the viral genome. These observations allow us to develop a new model for genome encapsidation and capsid assembly.

PubMed: 26657148
DOI: 10.1038/ncomms10113

実験手法

ELECTRON MICROSCOPY (3.44 Å)