3CNF

3.88 Angstrom structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy

3CNF の概要

• エントリーDOI: 10.2210/pdb3cnf/pdb
• EMDBエントリー: 1508
• 分子名称: VP1, VP3 (2 entities in total)
• 機能のキーワード: cytoplasmic polyhedrosis virus, capsid protein, turret protein, polyhedrin-binding domain, guanylyltransferase domain, icosahedral virus, virus
• 由来する生物種: Bombyx mori cypovirus 1; 詳細
• 細胞内の位置: Virion: Q6TS43
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 416868.83

構造登録者

Yu, X.,Jin, L.,Zhou, Z.H. (登録日: 2008-03-25, 公開日: 2008-04-29, 最終更新日: 2024-02-21)

主引用文献

Yu, X.,Jin, L.,Zhou, Z.H.
3.88 A structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy.
Nature, 453:415-419, 2008

PubMed Abstract: Cytoplasmic polyhedrosis virus (CPV) is unique within the Reoviridae family in having a turreted single-layer capsid contained within polyhedrin inclusion bodies, yet being fully capable of cell entry and endogenous RNA transcription. Biochemical data have shown that the amino-terminal 79 residues of the CPV turret protein (TP) is sufficient to bring CPV or engineered proteins into the polyhedrin matrix for micro-encapsulation. Here we report the three-dimensional structure of CPV at 3.88 A resolution using single-particle cryo-electron microscopy. Our map clearly shows the turns and deep grooves of alpha-helices, the strand separation in beta-sheets, and densities for loops and many bulky side chains; thus permitting atomic model-building effort from cryo-electron microscopy maps. We observed a helix-to-beta-hairpin conformational change between the two conformational states of the capsid shell protein in the region directly interacting with genomic RNA. We have also discovered a messenger RNA release hole coupled with the mRNA capping machinery unique to CPV. Furthermore, we have identified the polyhedrin-binding domain, a structure that has potential in nanobiotechnology applications.

PubMed: 18449192
DOI: 10.1038/nature06893

実験手法

ELECTRON MICROSCOPY (3.88 Å)