+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 3iyb | ||||||
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タイトル | Poliovirus early RNA-release intermediate | ||||||
要素 |
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キーワード | VIRAL PROTEIN / Picornavirus / poliovirus / intermediate / RNA release / 80S / ATP-binding / Capsid protein / Covalent protein-RNA linkage / Cytoplasmic vesicle / Helicase / Host-virus interaction / Hydrolase / Lipoprotein / Membrane / Myristate / Nucleotide-binding / Nucleotidyltransferase / Phosphoprotein / Protease / RNA replication / RNA-binding / RNA-directed RNA polymerase / Thiol protease / Transferase / Virion | ||||||
機能・相同性 | 機能・相同性情報 caveolin-mediated endocytosis of virus by host cell / symbiont-mediated suppression of host translation initiation / protein complex oligomerization / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / monoatomic ion channel activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane ...caveolin-mediated endocytosis of virus by host cell / symbiont-mediated suppression of host translation initiation / protein complex oligomerization / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / monoatomic ion channel activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / ribonucleoside triphosphate phosphatase activity / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / cytoplasmic vesicle membrane / endocytosis involved in viral entry into host cell / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport / DNA replication / RNA helicase activity / symbiont-mediated suppression of host innate immune response / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / DNA-templated transcription / host cell nucleus / virion attachment to host cell / structural molecule activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding 類似検索 - 分子機能 | ||||||
生物種 | Human poliovirus 1 Mahoney (ポリオウイルス) Poliovirus type 3 Human poliovirus 1 (ポリオウイルス) | ||||||
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: 10 Å | ||||||
データ登録者 | Levy, H.C. / Bostina, M. / Filman, D.J. / Hogle, J.M. | ||||||
引用 | ジャーナル: J Virol / 年: 2010 タイトル: Catching a virus in the act of RNA release: a novel poliovirus uncoating intermediate characterized by cryo-electron microscopy. 著者: Hazel C Levy / Mihnea Bostina / David J Filman / James M Hogle / 要旨: Poliovirus infection requires that the particle undergo a series of conformational transitions that lead to cell entry and genome release. In an effort to understand the conformational changes ...Poliovirus infection requires that the particle undergo a series of conformational transitions that lead to cell entry and genome release. In an effort to understand the conformational changes associated with the release of the RNA genome, we have used cryo-electron microscopy to characterize the structure of the 80S "empty" particles of poliovirus that are thought to represent the final product of the cell entry pathway. Using two-dimensional classification methods, we show that preparations of 80S particles contain at least two structures, which might represent snapshots from a continuous series of conformers. Using three-dimensional reconstruction methods, we have solved the structure of two distinct forms at subnanometric resolution, and we have built and refined pseudoatomic models into the reconstructions. The reconstructions and the derived models demonstrate that the two structural forms are both slightly expanded, resulting in partial disruption of interprotomer interfaces near their particle 2-fold axes, which may represent the site where RNA is released. The models demonstrate that each of the two 80S structures has undergone a unique set of movements of the capsid proteins, associated with rearrangement of flexible loops and amino-terminal extensions that participate in contacts between protomers, between pentamers, and with the viral RNA. | ||||||
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 | 3iyb.cif.gz | 38.5 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb3iyb.ent.gz | 18.7 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 3iyb.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 | 3iyb_validation.pdf.gz | 759 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 3iyb_full_validation.pdf.gz | 758.6 KB | 表示 | |
XML形式データ | 3iyb_validation.xml.gz | 15.8 KB | 表示 | |
CIF形式データ | 3iyb_validation.cif.gz | 22.5 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/iy/3iyb ftp://data.pdbj.org/pub/pdb/validation_reports/iy/3iyb | 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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2 |
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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)) |
-要素
#1: タンパク質 | 分子量: 26558.979 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) Human poliovirus 1 Mahoney (ポリオウイルス) 参照: UniProt: P03300, picornain 2A, nucleoside-triphosphate phosphatase, picornain 3C, RNA-directed RNA polymerase |
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#2: タンパク質・ペプチド | 分子量: 1518.665 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B) (ポリオウイルス) 参照: UniProt: P03302, picornain 2A, nucleoside-triphosphate phosphatase, picornain 3C, RNA-directed RNA polymerase |
#3: タンパク質 | 分子量: 25777.613 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) Human poliovirus 1 (ポリオウイルス) 参照: UniProt: Q9E912, UniProt: P03300*PLUS |
#4: タンパク質 | 分子量: 27181.639 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) Human poliovirus 1 Mahoney (ポリオウイルス) 参照: UniProt: P03300, picornain 2A, nucleoside-triphosphate phosphatase, picornain 3C, RNA-directed RNA polymerase |
#5: タンパク質・ペプチド | 分子量: 954.168 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) Human poliovirus 1 (ポリオウイルス) |
-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 | 名称: 80S poliovirus / タイプ: VIRUS 詳細: 60 promoters arranged as a icosahedron. native virus heat-treated at 56 degrees C 別称: poliovirus 1 mahoney |
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分子量 | 値: 8.3 MDa / 実験値: YES |
ウイルスについての詳細 | 中空か: YES / エンベロープを持つか: NO / ホストのカテゴリ: VERTEBRATES / 単離: SEROTYPE / タイプ: VIRION |
天然宿主 | 生物種: Homo sapiens |
緩衝液 | 名称: 20mM Tris pH 7.4, 2mM CaCl2, 20mM NaCl / pH: 7.4 / 詳細: 20mM Tris pH 7.4, 2mM CaCl2, 20mM NaCl |
試料 | 濃度: 0.2 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES / 詳細: 20mM Tris, 50mM NaCl, 2 mM CaCl2 |
急速凍結 | 装置: HOMEMADE PLUNGER / 凍結剤: ETHANE / 手法: blot for 3 secs |
-電子顕微鏡撮影
実験機器 | モデル: Tecnai F30 / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI TECNAI F30 |
電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 200 kV / 照射モード: OTHER |
電子レンズ | モード: OTHER / 倍率(公称値): 59000 X / 最大 デフォーカス(公称値): 3 nm / 最小 デフォーカス(公称値): 0.9 nm / カメラ長: 0 mm |
試料ホルダ | 試料ホルダーモデル: GATAN LIQUID NITROGEN / 資料ホルダタイプ: Eucentric / 傾斜角・最大: 0 ° / 傾斜角・最小: 0 ° |
撮影 | 電子線照射量: 15 e/Å2 / フィルム・検出器のモデル: KODAK SO-163 FILM |
-解析
EMソフトウェア |
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CTF補正 | 詳細: each micrograph | ||||||||||||||||||||
対称性 | 点対称性: I (正20面体型対称) | ||||||||||||||||||||
3次元再構成 | 手法: PFT / 解像度: 10 Å / 解像度の算出法: FSC 0.5 CUT-OFF 詳細: Details about the particle: 10,000 particle were partitioned into two distinct classes 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 / 詳細: REFINEMENT PROTOCOL--Rigid Body | ||||||||||||||||||||
原子モデル構築 | PDB-ID: 1POV Accession code: 1POV / Source name: PDB / タイプ: experimental model | ||||||||||||||||||||
精密化ステップ | サイクル: LAST
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