- PDB-2xyz: De Novo model of Bacteriophage P22 virion coat protein -
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基本情報
登録情報
データベース: PDB / ID: 2xyz
タイトル
De Novo model of Bacteriophage P22 virion coat protein
要素
COAT PROTEIN
キーワード
VIRUS / MATURATION / DSDNA VIRUS
機能・相同性
Major capsid protein Gp5 / P22 coat protein - gene protein 5 / viral procapsid / viral procapsid maturation / T=7 icosahedral viral capsid / viral capsid / identical protein binding / Major capsid protein / Major capsid protein
ジャーナル: Proc Natl Acad Sci U S A / 年: 2011 タイトル: Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus. 著者: Dong-Hua Chen / Matthew L Baker / Corey F Hryc / Frank DiMaio / Joanita Jakana / Weimin Wu / Matthew Dougherty / Cameron Haase-Pettingell / Michael F Schmid / Wen Jiang / David Baker / ...著者: Dong-Hua Chen / Matthew L Baker / Corey F Hryc / Frank DiMaio / Joanita Jakana / Weimin Wu / Matthew Dougherty / Cameron Haase-Pettingell / Michael F Schmid / Wen Jiang / David Baker / Jonathan A King / Wah Chiu / 要旨: Formation of many dsDNA viruses begins with the assembly of a procapsid, containing scaffolding proteins and a multisubunit portal but lacking DNA, which matures into an infectious virion. This ...Formation of many dsDNA viruses begins with the assembly of a procapsid, containing scaffolding proteins and a multisubunit portal but lacking DNA, which matures into an infectious virion. This process, conserved among dsDNA viruses such as herpes viruses and bacteriophages, is key to forming infectious virions. Bacteriophage P22 has served as a model system for this study in the past several decades. However, how capsid assembly is initiated, where and how scaffolding proteins bind to coat proteins in the procapsid, and the conformational changes upon capsid maturation still remain elusive. Here, we report Cα backbone models for the P22 procapsid and infectious virion derived from electron cryomicroscopy density maps determined at 3.8- and 4.0-Å resolution, respectively, and the first procapsid structure at subnanometer resolution without imposing symmetry. The procapsid structures show the scaffolding protein interacting electrostatically with the N terminus (N arm) of the coat protein through its C-terminal helix-loop-helix motif, as well as unexpected interactions between 10 scaffolding proteins and the 12-fold portal located at a unique vertex. These suggest a critical role for the scaffolding proteins both in initiating the capsid assembly at the portal vertex and propagating its growth on a T = 7 icosahedral lattice. Comparison of the procapsid and the virion backbone models reveals coordinated and complex conformational changes. These structural observations allow us to propose a more detailed molecular mechanism for the scaffolding-mediated capsid assembly initiation including portal incorporation, release of scaffolding proteins upon DNA packaging, and maturation into infectious virions.
モード: BRIGHT FIELD / 倍率(公称値): 60000 X / 倍率(補正後): 60000 X / 最大 デフォーカス(公称値): 2300 nm / 最小 デフォーカス(公称値): 300 nm / Cs: 1.6 mm
試料ホルダ
温度: 4.2 K
撮影
電子線照射量: 36 e/Å2 / フィルム・検出器のモデル: KODAK SO-163 FILM
画像スキャン
デジタル画像の数: 1262
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解析
EMソフトウェア
名称: EMAN / カテゴリ: 3次元再構成
CTF補正
詳細: EACH PARTICLE
対称性
点対称性: I (正20面体型対称)
3次元再構成
手法: FOURIER METHODS / 解像度: 4 Å / 粒子像の数: 18300 / ピクセルサイズ(公称値): 1.06 Å / ピクセルサイズ(実測値): 1.06 Å 詳細: MAKE3D IN EMAN. C-TERMINAL 5 RESIDUES WERE NOT MODELE MODELED SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-1826. 対称性のタイプ: POINT
原子モデル構築
プロトコル: OTHER / 空間: REAL / Target criteria: FSC / 詳細: REFINEMENT PROTOCOL--EM