+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 3j2m | ||||||
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タイトル | The X-ray structure of the gp15 hexamer and the model of the gp18 protein fitted into the cryo-EM reconstruction of the extended T4 tail | ||||||
要素 |
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キーワード | VIRAL PROTEIN / bacteriophage T4 / phage tail terminator protein / phage sheath protein | ||||||
機能・相同性 | 機能・相同性情報 virus tail, sheath / symbiont genome ejection through host cell envelope, contractile tail mechanism / virion component 類似検索 - 分子機能 | ||||||
生物種 | Enterobacteria phage T4 (ファージ) | ||||||
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: 15 Å | ||||||
データ登録者 | Fokine, A. / Zhang, Z. / Kanamaru, S. / Bowman, V.D. / Aksyuk, A. / Arisaka, F. / Rao, V.B. / Rossmann, M.G. | ||||||
引用 | ジャーナル: J Mol Biol / 年: 2013 タイトル: The molecular architecture of the bacteriophage T4 neck. 著者: Andrei Fokine / Zhihong Zhang / Shuji Kanamaru / Valorie D Bowman / Anastasia A Aksyuk / Fumio Arisaka / Venigalla B Rao / Michael G Rossmann / 要旨: A hexamer of the bacteriophage T4 tail terminator protein, gp15, attaches to the top of the phage tail stabilizing the contractile sheath and forming the interface for binding of the independently ...A hexamer of the bacteriophage T4 tail terminator protein, gp15, attaches to the top of the phage tail stabilizing the contractile sheath and forming the interface for binding of the independently assembled head. Here we report the crystal structure of the gp15 hexamer, describe its interactions in T4 virions that have either an extended tail or a contracted tail, and discuss its structural relationship to other phage proteins. The neck of T4 virions is decorated by the "collar" and "whiskers", made of fibritin molecules. Fibritin acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. The collar and whiskers are environment-sensing devices, regulating the retraction of the long tail fibers under unfavorable conditions, thus preventing infection. Cryo-electron microscopy analysis suggests that twelve fibritin molecules attach to the phage neck with six molecules forming the collar and six molecules forming the whiskers. #1: ジャーナル: Nat Struct Mol Biol / 年: 2005 タイトル: The tail structure of bacteriophage T4 and its mechanism of contraction. 著者: Victor A Kostyuchenko / Paul R Chipman / Petr G Leiman / Fumio Arisaka / Vadim V Mesyanzhinov / Michael G Rossmann / 要旨: Bacteriophage T4 and related viruses have a contractile tail that serves as an efficient mechanical device for infecting bacteria. A three-dimensional cryo-EM reconstruction of the mature T4 tail ...Bacteriophage T4 and related viruses have a contractile tail that serves as an efficient mechanical device for infecting bacteria. A three-dimensional cryo-EM reconstruction of the mature T4 tail assembly at 15-A resolution shows the hexagonal dome-shaped baseplate, the extended contractile sheath, the long tail fibers attached to the baseplate and the collar formed by six whiskers that interact with the long tail fibers. Comparison with the structure of the contracted tail shows that tail contraction is associated with a substantial rearrangement of the domains within the sheath protein and results in shortening of the sheath to about one-third of its original length. During contraction, the tail tube extends beneath the baseplate by about one-half of its total length and rotates by 345 degrees , allowing it to cross the host's periplasmic space. | ||||||
履歴 |
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-構造の表示
ムービー |
ムービービューア |
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構造ビューア | 分子: MolmilJmol/JSmol |
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 3j2m.cif.gz | 914.7 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb3j2m.ent.gz | 759.8 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 3j2m.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 3j2m_validation.pdf.gz | 849.3 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 3j2m_full_validation.pdf.gz | 1.1 MB | 表示 | |
XML形式データ | 3j2m_validation.xml.gz | 163.7 KB | 表示 | |
CIF形式データ | 3j2m_validation.cif.gz | 244.4 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/j2/3j2m ftp://data.pdbj.org/pub/pdb/validation_reports/j2/3j2m | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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-要素
#1: タンパク質 | 分子量: 31587.486 Da / 分子数: 6 / 由来タイプ: 組換発現 由来: (組換発現) Enterobacteria phage T4 (ファージ) 遺伝子: 15 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P11112 #2: タンパク質 | 分子量: 71289.484 Da / 分子数: 6 / Mutation: R510P / 由来タイプ: 組換発現 由来: (組換発現) Enterobacteria phage T4 (ファージ) 遺伝子: 18 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P13332 配列の詳細 | THE AUTHORS STATE THAT D100E, G148A, N150I, Y151I, E301G, A399V, AND H454Y ARE NATURAL VARIANTS AS ...THE AUTHORS STATE THAT D100E, G148A, N150I, Y151I, E301G, A399V, AND H454Y ARE NATURAL VARIANTS AS PER PDB ENTRY 3FOA. | |
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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 |
-試料調製
構成要素 |
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緩衝液 | pH: 7 | ||||||||||||||||||||
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||||
試料支持 | 詳細: 200 mesh copper grids | ||||||||||||||||||||
急速凍結 | 凍結剤: ETHANE |
-電子顕微鏡撮影
顕微鏡 | モデル: FEI/PHILIPS CM300FEG/ST / 日付: 2003年1月10日 |
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電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: SPOT SCAN |
電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 45000 X / 倍率(補正後): 47000 X / 最大 デフォーカス(公称値): 4000 nm / 最小 デフォーカス(公称値): 1000 nm / Cs: 2 mm |
試料ホルダ | 試料ホルダーモデル: GATAN LIQUID NITROGEN |
画像スキャン | デジタル画像の数: 89 |
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 |
-解析
EMソフトウェア |
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CTF補正 | 詳細: each particle image | ||||||||||||
対称性 | 点対称性: C6 (6回回転対称) | ||||||||||||
3次元再構成 | 解像度: 15 Å / 解像度の算出法: FSC 0.5 CUT-OFF / 粒子像の数: 3029 / ピクセルサイズ(公称値): 3.97 Å / ピクセルサイズ(実測値): 3.97 Å 詳細: reconstruction done with in-house implementation of BP RP algorithm from SPIDER to support non-cubic reconstruction volumes 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: REAL / 詳細: REFINEMENT PROTOCOL--rigid body | ||||||||||||
精密化ステップ | サイクル: LAST
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