7VFD

Cryo-EM structure of Vaccinia virus scaffolding protein D13

7VFD の概要

• エントリーDOI: 10.2210/pdb7vfd/pdb
• EMDBエントリー: 31949
• 分子名称: Scaffold protein D13 (2 entities in total)
• 機能のキーワード: scaffold, capsid, double-jelly-roll, viral protein
• 由来する生物種: Vaccinia virus (strain Western Reserve) (VACV, Vaccinia virus (strain WR))
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 185028.96

構造登録者

Wolf, M.,Hyun, J.,Matsunami, H.,Kim, T.G. (登録日: 2021-09-13, 公開日: 2022-02-23, 最終更新日: 2024-06-19)

主引用文献

Hyun, J.,Matsunami, H.,Kim, T.G.,Wolf, M.
Assembly mechanism of the pleomorphic immature poxvirus scaffold.
Nat Commun, 13:1704-1704, 2022

PubMed Abstract: In Vaccinia virus (VACV), the prototype poxvirus, scaffold protein D13 forms a honeycomb-like lattice on the viral membrane that results in formation of the pleomorphic immature virion (IV). The structure of D13 is similar to those of major capsid proteins that readily form icosahedral capsids in nucleocytoplasmic large DNA viruses (NCLDVs). However, the detailed assembly mechanism of the nonicosahedral poxvirus scaffold has never been understood. Here we show the cryo-EM structures of the D13 trimer and scaffold intermediates produced in vitro. The structures reveal that the displacement of the short N-terminal α-helix is critical for initiation of D13 self-assembly. The continuous curvature of the IV is mediated by electrostatic interactions that induce torsion between trimers. The assembly mechanism explains the semiordered capsid-like arrangement of D13 that is distinct from icosahedral NCLDVs. Our structures explain how a single protein can self-assemble into different capsid morphologies and represent a local exception to the universal Caspar-Klug theory of quasi-equivalence.

PubMed: 35361762
DOI: 10.1038/s41467-022-29305-5

実験手法

ELECTRON MICROSCOPY (2.25 Å)