8OPA

Virus-like Particle based on PVY coat protein with stacked-ring architecture

これはPDB形式変換不可エントリーです。

8OPA の概要

• エントリーDOI: 10.2210/pdb8opa/pdb
• 関連するPDBエントリー: 6HXZ 8OPB
• EMDBエントリー: 0298 17046 17047
• 分子名称: Genome polyprotein (Fragment) (1 entity in total)
• 機能のキーワード: stacked-ring, vlp, potyvirus, pvy, virus like particle
• 由来する生物種: Potato virus Y strain NTN
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 718459.13

構造登録者

Kavcic, L.,Kezar, A.,Podobnik, M. (登録日: 2023-04-07, 公開日: 2024-01-24, 最終更新日: 2024-01-31)

主引用文献

Kavcic, L.,Kezar, A.,Koritnik, N.,Znidaric, M.T.,Klobucar, T.,Vicic, Z.,Merzel, F.,Holden, E.,Benesch, J.L.P.,Podobnik, M.
From structural polymorphism to structural metamorphosis of the coat protein of flexuous filamentous potato virus Y.
Commun Chem, 7:14-14, 2024

PubMed Abstract: The structural diversity and tunability of the capsid proteins (CPs) of various icosahedral and rod-shaped viruses have been well studied and exploited in the development of smart hybrid nanoparticles. However, the potential of CPs of the wide-spread flexuous filamentous plant viruses remains to be explored. Here, we show that we can control the shape, size, RNA encapsidation ability, symmetry, stability and surface functionalization of nanoparticles through structure-based design of CP from potato virus Y (PVY). We provide high-resolution insight into CP-based self-assemblies, ranging from large polymorphic or monomorphic filaments to smaller annular, cubic or spherical particles. Furthermore, we show that we can prevent CP self-assembly in bacteria by fusion with a cleavable protein, enabling controlled nanoparticle formation in vitro. Understanding the remarkable structural diversity of PVY CP not only provides possibilities for the production of biodegradable nanoparticles, but may also advance future studies of CP's polymorphism in a biological context.

PubMed: 38233506
DOI: 10.1038/s42004-024-01100-x

実験手法

ELECTRON MICROSCOPY (3.34 Å)