- PDB-3iyh: P22 procapsid coat protein structures reveal a novel mechanism fo... -
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基本情報
登録情報
データベース: PDB / ID: 3iyh
タイトル
P22 procapsid coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical cross-links
要素
Coat protein
キーワード
VIRUS / HK97-like fold / Capsid protein / Late protein / Virion
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
ジャーナル: Structure / 年: 2010 タイトル: P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks. 著者: Kristin N Parent / Reza Khayat / Long H Tu / Margaret M Suhanovsky / Juliana R Cortines / Carolyn M Teschke / John E Johnson / Timothy S Baker / 要旨: Viral capsid assembly and stability in tailed, dsDNA phage and Herpesviridae are achieved by various means including chemical crosslinks (unique to HK97), or auxiliary proteins (lambda, T4, phi29, ...Viral capsid assembly and stability in tailed, dsDNA phage and Herpesviridae are achieved by various means including chemical crosslinks (unique to HK97), or auxiliary proteins (lambda, T4, phi29, and herpesviruses). All these viruses have coat proteins (CP) with a conserved, HK97-like core structure. We used a combination of trypsin digestion, gold labeling, cryo-electron microscopy, 3D image reconstruction, and comparative modeling to derive two independent, pseudoatomic models of bacteriophage P22 CP: before and after maturation. P22 capsid stabilization results from intersubunit interactions among N-terminal helices and an extensive "P loop," which obviate the need for crosslinks or auxiliary proteins. P22 CP also has a telokin-like Ig domain that likely stabilizes the monomer fold so that assembly may proceed via individual subunit addition rather than via preformed capsomers as occurs in HK97. Hence, the P22 CP structure may be a paradigm for understanding how monomers assemble in viruses like phi29 and HSV-1.
モード: BRIGHT FIELD / 倍率(公称値): 39000 X / 最大 デフォーカス(公称値): 3160 nm / 最小 デフォーカス(公称値): 630 nm / Cs: 2.3 mm / 非点収差: at working magnification / カメラ長: 0 mm
試料ホルダ
試料ホルダーモデル: OTHER / 資料ホルダタイプ: Polara Multi Specimen Holder / 温度: 90 K / 最高温度: 90 K / 最低温度: 90 K / 傾斜角・最大: -9999 ° / 傾斜角・最小: -9999 °
撮影
電子線照射量: 8 e/Å2 / フィルム・検出器のモデル: KODAK SO-163 FILM
放射
プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray
放射波長
相対比: 1
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解析
EMソフトウェア
ID
名称
カテゴリ
1
Coot
モデルフィッティング
2
MODELLER
モデルフィッティング
3
Auto3DEM
3次元再構成
CTF補正
詳細: ROBEM
対称性
点対称性: I (正20面体型対称)
3次元再構成
手法: iterative model-based procedure / 解像度: 8.2 Å / 解像度の算出法: FSC 0.5 CUT-OFF / 粒子像の数: 3308 / ピクセルサイズ(公称値): 1.795 Å / ピクセルサイズ(実測値): 1.795 Å 詳細: Final map was calculated at 7.0A resolution ( Details about the particle: data were collected on film ) 対称性のタイプ: POINT
原子モデル構築
ID
プロトコル
空間
Target criteria
詳細
1
FLEXIBLEFIT
REAL
cross-correlation coefficient
METHOD--local refinement, flexible fitting REFINEMENT PROTOCOL--rigid body