1JMU

Crystal Structure of the Reovirus mu1/sigma3 Complex

1JMU の概要

• エントリーDOI: 10.2210/pdb1jmu/pdb
• 分子名称: PROTEIN MU-1, SIGMA 3 PROTEIN, CHLORIDE ION, ... (8 entities in total)
• 機能のキーワード: protein-protein complex, jelly roll, zinc finger, viral protein
• 由来する生物種: Reovirus sp.; 詳細
• 細胞内の位置: Outer capsid protein mu-1: Virion: P11077 P11077
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 354462.25

構造登録者

Liemann, S.,Nibert, M.L.,Harrison, S.C. (登録日: 2001-07-20, 公開日: 2002-02-06, 最終更新日: 2024-10-30)

主引用文献

Liemann, S.,Chandran, K.,Baker, T.S.,Nibert, M.L.,Harrison, S.C.
Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3.
Cell(Cambridge,Mass.), 108:283-295, 2002

PubMed Abstract: Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, Mu1. The structure of Mu1, complexed with its "protector" protein, Sigma3, and the fit of this Mu1(3)Sigma3(3) heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides Mu1 into myristoylated Mu1N and Mu1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of Mu1N, linked to a major conformational change of the entire Mu1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of Mu1N, and long-range molecular rearrangement of Mu1C, thus appears to be part of the penetration mechanism.

PubMed: 11832217
DOI: 10.1016/S0092-8674(02)00612-8

実験手法

X-RAY DIFFRACTION (2.8 Å)