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基本情報
登録情報 | データベース: PDB / ID: 3ddx | ||||||
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タイトル | HK97 bacteriophage capsid Expansion Intermediate-II model | ||||||
![]() | Major capsid protein | ||||||
![]() | VIRUS / Bacteriophage / HK97 / Capsid Protein / Expansion Intermediate / Virion / icosahedral virus | ||||||
機能・相同性 | : / Phage capsid / Phage capsid family / viral procapsid maturation / T=7 icosahedral viral capsid / viral capsid / identical protein binding / Major capsid protein![]() | ||||||
生物種 | ![]() | ||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 14 Å | ||||||
![]() | Lee, K.K. / Gan, L. / Conway, J.F. / Hendrix, R.W. / Steven, A.C. / Johnson, J.E. | ||||||
![]() | ![]() タイトル: Virus capsid expansion driven by the capture of mobile surface loops. 著者: Kelly K Lee / Lu Gan / Hiro Tsuruta / Crystal Moyer / James F Conway / Robert L Duda / Roger W Hendrix / Alasdair C Steven / John E Johnson / ![]() 要旨: The capsids of tailed-DNA bacteriophages first assemble as procapsids, which mature by converting into a new form that is strong enough to contain a densely packed viral chromosome. We demonstrate ...The capsids of tailed-DNA bacteriophages first assemble as procapsids, which mature by converting into a new form that is strong enough to contain a densely packed viral chromosome. We demonstrate that the intersubunit crosslinking that occurs during maturation of HK97 capsids actually promotes the structural transformation. Small-angle X-ray scattering and crosslinking assays reveal that a shift in the crosslink pattern accompanies conversion of a semimature particle, Expansion Intermediate-I/II, to a more mature state, Balloon. This transition occurs in a switch-like fashion. We find that crosslink formation shifts the global conformational balance to favor the balloon state. A pseudoatomic model of EI-I/II derived from cryo-EM provides insight into the relationship between crosslink formation and conformational switching. | ||||||
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構造の表示
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構造ビューア | 分子: ![]() ![]() |
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-検証レポート
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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対称性 | 点対称性: (シェーンフリース記号: I (正20面体型対称)) |
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要素
#1: タンパク質 | 分子量: 30804.607 Da / 分子数: 7 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() Has protein modification | N | |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
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試料調製
構成要素 | 名称: Bacteriophage HK97 Expansion Intermediate II / タイプ: VIRUS |
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緩衝液 | 名称: 50mM Na-Acetate, 200mM KCl / pH: 4.18 / 詳細: 50mM Na-Acetate, 200mM KCl |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
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電子顕微鏡撮影
顕微鏡 | モデル: FEI/PHILIPS CM200FEG |
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電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 38000 X |
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解析
EMソフトウェア |
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対称性 | 点対称性: I (正20面体型対称) | ||||||||||||
3次元再構成 | 解像度: 14 Å / 対称性のタイプ: POINT | ||||||||||||
原子モデル構築 | プロトコル: RIGID BODY FIT / 空間: RECIPROCAL / Target criteria: Vector Reciprocal Space Target 詳細: METHOD--manual and rigid body fitting. THE COORDINATES CONTAIN ONLY THE BACKBONE ATOMS. DURING RIGID BODY DOCKING OF THE PROTEIN MODEL INTO THE EM DENSITY, THE TWO SUBDOMAINS 104-125 AND 155- ...詳細: METHOD--manual and rigid body fitting. THE COORDINATES CONTAIN ONLY THE BACKBONE ATOMS. DURING RIGID BODY DOCKING OF THE PROTEIN MODEL INTO THE EM DENSITY, THE TWO SUBDOMAINS 104-125 AND 155-175 OF EACH SUBUNIT WERE ALLOWED TO MOVE INDEPENDENTLY FROM THE REMAINDER OF THE RESIDUES (THE CORE OF EACH SUBUNIT). THAT IS WHY THE CONNECTIVITY OF THOSE SEGMENTS WITH THE REST OF THE SUBUNIT IS NOT WELL-PRESERVED. REFINEMENT PROTOCOL--Rigid Body, Magnification Optimized using Van Der Waals Constraints and Real-space Correlation Coefficient | ||||||||||||
原子モデル構築 | PDB-ID: 1OHG Accession code: 1OHG / Source name: PDB / タイプ: experimental model | ||||||||||||
精密化ステップ | サイクル: LAST
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