3IYL

Atomic CryoEM Structure of a Nonenveloped Virus Suggests How Membrane Penetration Protein is Primed for Cell Entry

3IYL の概要

• エントリーDOI: 10.2210/pdb3iyl/pdb
• EMDBエントリー: 5160
• 分子名称: Outer capsid VP4, Core protein VP6, VP1, ... (5 entities in total)
• 機能のキーワード: non-enveloped virus, membrane penetration protein, autocleavage, myristol group, icosahedral virus, virus
• 由来する生物種: Grass carp reovirus; 詳細
• タンパク質・核酸の鎖数: 25
• 化学式量合計: 1870350.56

構造登録者

Zhang, X.,Jin, L.,Fang, Q.,Hui, W.,Zhou, Z.H. (登録日: 2010-02-02, 公開日: 2010-05-12, 最終更新日: 2024-11-20)

主引用文献

Zhang, X.,Jin, L.,Fang, Q.,Hui, W.H.,Zhou, Z.H.
3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry.
Cell(Cambridge,Mass.), 141:472-482, 2010

PubMed Abstract: To achieve cell entry, many nonenveloped viruses must transform from a dormant to a primed state. In contrast to the membrane fusion mechanism of enveloped viruses (e.g., influenza virus), this membrane penetration mechanism is poorly understood. Here, using single-particle cryo-electron microscopy, we report a 3.3 A structure of the primed, infectious subvirion particle of aquareovirus. The density map reveals side-chain densities of all types of amino acids (except glycine), enabling construction of a full-atom model of the viral particle. Our structure and biochemical results show that priming involves autocleavage of the membrane penetration protein and suggest that Lys84 and Glu76 may facilitate this autocleavage in a nucleophilic attack. We observe a myristoyl group, covalently linked to the N terminus of the penetration protein and embedded in a hydrophobic pocket. These results suggest a well-orchestrated process of nonenveloped virus entry involving autocleavage of the penetration protein prior to exposure of its membrane-insertion finger.

PubMed: 20398923
DOI: 10.1016/j.cell.2010.03.041

実験手法

ELECTRON MICROSCOPY (3.3 Å)