4DOX

Crystal Structure of Papaya mosaic virus capsid protein

4DOX の概要

• エントリーDOI: 10.2210/pdb4dox/pdb
• 分子名称: Coat protein (2 entities in total)
• 機能のキーワード: all helix capsid protein, virus capsid structure, viral protein
• 由来する生物種: Papaya mosaic virus (PMV)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48792.85

構造登録者

Wang, T.,Li, H. (登録日: 2012-02-11, 公開日: 2012-06-13, 最終更新日: 2024-02-28)

主引用文献

Yang, S.,Wang, T.,Bohon, J.,Gagne, N.,Bolduc, M.,Leclerc, D.,Li, H.
Crystal structure of the coat protein of the flexible filamentous papaya mosaic virus.
J.Mol.Biol., 422:263-273, 2012

PubMed Abstract: Papaya mosaic virus (PapMV) is a filamentous plant virus that belongs to the Alphaflexiviridae family. Flexible filamentous viruses have defied more than two decades of effort in fiber diffraction, and no high-resolution structure is available for any member of the Alphaflexiviridae family. Here, we report our structural characterization of PapMV by X-ray crystallography and cryo-electron microscopy three-dimensional reconstruction. We found that PapMV is 135Å in diameter with a helical symmetry of ~10 subunits per turn. Crystal structure of the C-terminal truncated PapMV coat protein (CP) reveals a novel all-helix fold with seven α-helices. Thus, the PapMVCP structure is different from the four-helix-bundle fold of tobacco mosaic virus in which helix bundling dominates the subunit interface in tobacco mosaic virus and conveys rigidity to the rod virus. PapMV CP was crystallized as an asymmetrical dimer in which one protein lassoes the other by the N-terminal peptide. Mutation of residues critical to the inter-subunit lasso interaction abolishes CP polymerization. The crystal structure suggests that PapMV may polymerize via the consecutive N-terminal loop lassoing mechanism. The structure of PapMV will be useful for rational design and engineering of the PapMV nanoparticles into innovative vaccines.

PubMed: 22659319
DOI: 10.1016/j.jmb.2012.05.032

実験手法

X-RAY DIFFRACTION (2.7 Å)