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データを開く
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基本情報
| 登録情報 | データベース: PDB / ID: 8sup | ||||||||||||||||||
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| タイトル | Structure of the 48S translation initiation complex assembled on the encephalomyocarditis virus IRES | ||||||||||||||||||
要素 |
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キーワード | RIBOSOME / EMCV / IRES / Cryo-EM / 40SIC | ||||||||||||||||||
| 機能・相同性 | 機能・相同性情報viral translational termination-reinitiation / eukaryotic translation initiation factor 3 complex, eIF3e / eukaryotic translation initiation factor 3 complex, eIF3m / IRES-dependent viral translational initiation / translation reinitiation / formation of cytoplasmic translation initiation complex / multi-eIF complex / eukaryotic translation initiation factor 3 complex / eukaryotic 43S preinitiation complex / translation factor activity, RNA binding ...viral translational termination-reinitiation / eukaryotic translation initiation factor 3 complex, eIF3e / eukaryotic translation initiation factor 3 complex, eIF3m / IRES-dependent viral translational initiation / translation reinitiation / formation of cytoplasmic translation initiation complex / multi-eIF complex / eukaryotic translation initiation factor 3 complex / eukaryotic 43S preinitiation complex / translation factor activity, RNA binding / eukaryotic 48S preinitiation complex / regulation of translational initiation / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / metal-dependent deubiquitinase activity / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / laminin receptor activity / Translation initiation complex formation / Formation of a pool of free 40S subunits / 90S preribosome / ubiquitin ligase inhibitor activity / positive regulation of signal transduction by p53 class mediator / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / phagocytic cup / translation regulator activity / rough endoplasmic reticulum / ribosomal small subunit export from nucleus / laminin binding / translation initiation factor binding / gastrulation / translation initiation factor activity / MDM2/MDM4 family protein binding / cytosolic ribosome / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / DNA-(apurinic or apyrimidinic site) lyase / ribosome assembly / positive regulation of translation / positive regulation of apoptotic signaling pathway / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / maturation of SSU-rRNA / small-subunit processome / translational initiation / PML body / spindle / fibrillar center / metallopeptidase activity / rRNA processing / positive regulation of canonical Wnt signaling pathway / rhythmic process / regulation of translation / ribosomal small subunit assembly / virus receptor activity / ribosome binding / ribosomal small subunit biogenesis / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / perikaryon / cytoplasmic translation / cell differentiation / tRNA binding / cysteine-type deubiquitinase activity / mitochondrial inner membrane / postsynaptic density / rRNA binding / structural constituent of ribosome / ribosome / translation / ribonucleoprotein complex / cell division / DNA repair / mRNA binding / apoptotic process / centrosome / synapse / dendrite / nucleolus / perinuclear region of cytoplasm / Golgi apparatus / DNA binding / RNA binding / zinc ion binding / nucleoplasm / membrane / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol 類似検索 - 分子機能 | ||||||||||||||||||
| 生物種 | ![]() Homo sapiens (ヒト) Encephalomyocarditis virus (脳心筋炎ウイルス) | ||||||||||||||||||
| 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: 3.1 Å | ||||||||||||||||||
データ登録者 | Bhattacharjee, S. / Abaeva, I.S. / Brown, Z.P. / Arhab, Y. / Fallah, H. / Jeevan, J.C. / Hellen, C.U.T. / Frank, J. / Pestova, T.V. | ||||||||||||||||||
| 資金援助 | 米国, 5件
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引用 | ジャーナル: EMBO J / 年: 2026タイトル: The mechanism of ribosomal recruitment during translation initiation on the Type 2 encephalomyocarditis virus IRES. 著者: Sayan Bhattacharjee / Irina S Abaeva / Zuben P Brown / Yani Arhab / Hengameh Fallah / Christopher U T Hellen / Joachim Frank / Tatyana V Pestova / ![]() 要旨: The encephalomyocarditis virus (EMCV) internal ribosomal entry side (IRES) and other Type 2 IRESs favor translation of the viral genome during infection. The domains H-L of these IRESs specifically ...The encephalomyocarditis virus (EMCV) internal ribosomal entry side (IRES) and other Type 2 IRESs favor translation of the viral genome during infection. The domains H-L of these IRESs specifically interact with the cellular translation initiation factors eIF4G/eIF4A through their essential JK domain. However, the JK domain is not sufficient for IRES activity, which also strictly requires the preceding domain I of unknown function. To identify interactions that drive ribosomal attachment to eIF4G/eIF4A-bound Type 2 IRESs, we determined the cryo-EM structure of 48S initiation complexes formed on the EMCV IRES. The apical cloverleaf of domain I contacts ribosomal proteins uS13 and uS19 via its subdomain Id, whereas the essential GNRA tetraloop in subdomain Ic interacts with the TψC domain of initiator tRNA. The IRES-tRNA interaction also provides a mechanism for release of the IRES after eIF2 is replaced by eIF5B during subunit joining to allow attachment of 60S subunits. Functional assays supported the exceptional role of these interactions for initiation on this IRES. The strong conservation of the apex of domain I amongst Type 2 IRESs suggests that the reported interactions provide a common general mechanism of ribosomal attachment on them all. #1: ジャーナル: bioRxiv / 年: 2025 タイトル: The mechanism of ribosomal recruitment during translation initiation on Type 2 IRESs. 著者: Sayan Bhattacharjee / Irina S Abaeva / Zuben P Brown / Yani Arhab / Hengameh Fallah / Christopher U T Hellen / Joachim Frank / Tatyana V Pestova / ![]() 要旨: The encephalomyocarditis virus (EMCV) IRES and other Type 2 IRESs comprise domains H-L and specifically interact with eIF4G/eIF4A through their essential JK domain. However, the JK domain is not ...The encephalomyocarditis virus (EMCV) IRES and other Type 2 IRESs comprise domains H-L and specifically interact with eIF4G/eIF4A through their essential JK domain. However, the JK domain is not sufficient for IRES function, which also requires the preceding domain I of unknown function. To identify interactions that drive ribosomal recruitment of eIF4G/eIF4A-bound Type 2 IRESs, we determined the cryo-EM structure of 48S initiation complexes formed on the EMCV IRES. It revealed that the apical domain I cloverleaf contacts ribosomal proteins uS13 and uS19 via its Id subdomain and that the essential GNRA tetraloop in subdomain Ic interacts directly with the TψC domain of initiator tRNA. Functional assays supported the exceptional role of these interactions for initiation on this IRES. The strong conservation of primary and secondary structures of the apex of domain I among Type 2 IRESs suggests that the reported interactions are a common essential feature of them all. | ||||||||||||||||||
| 履歴 |
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構造の表示
| 構造ビューア | 分子: Molmil Jmol/JSmol |
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ダウンロードとリンク
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ダウンロード
| PDBx/mmCIF形式 | 8sup.cif.gz | 2.4 MB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb8sup.ent.gz | 表示 | PDB形式 | |
| PDBx/mmJSON形式 | 8sup.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
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/su/8sup ftp://data.pdbj.org/pub/pdb/validation_reports/su/8sup | HTTPS FTP |
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-関連構造データ
| 関連構造データ | ![]() 40774MC M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 ( |
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| 類似構造データ | 類似検索 - 機能・相同性 F&H 検索 |
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リンク
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集合体
| 登録構造単位 | ![]()
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要素
-Eukaryotic translation initiation factor ... , 10種, 10分子 opqrstuvAj
| #1: タンパク質 | 分子量: 164902.656 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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| #2: タンパク質 | 分子量: 97923.547 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
| #3: タンパク質 | 分子量: 52281.633 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
| #4: タンパク質 | 分子量: 37846.730 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
| #5: タンパク質 | 分子量: 39952.281 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
| #6: タンパク質 | 分子量: 25129.709 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
| #7: タンパク質 | 分子量: 66804.766 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
| #8: タンパク質 | 分子量: 42555.832 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
| #11: タンパク質 | 分子量: 16488.449 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: EIF1AX, EIF1A, EIF4C / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: P47813 |
| #46: タンパク質 | 分子量: 36161.180 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
-RNA鎖 , 3種, 3分子 23i
| #9: RNA鎖 | 分子量: 603100.938 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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| #10: RNA鎖 | 分子量: 28627.121 Da / 分子数: 1 / 由来タイプ: 天然 由来: (天然) Encephalomyocarditis virus (脳心筋炎ウイルス)参照: GenBank: 485965777 |
| #45: RNA鎖 | 分子量: 24231.510 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
+タンパク質 , 33種, 33分子 BCDEFGHIJKLMNOPQRSTUVWXYZabcde...
-タンパク質・ペプチド / 非ポリマー , 2種, 2分子 n

| #47: タンパク質・ペプチド | 分子量: 3473.451 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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| #48: 化合物 | ChemComp-ZN / |
-詳細
| 研究の焦点であるリガンドがあるか | N |
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| Has protein modification | Y |
-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: CELL / 3次元再構成法: 単粒子再構成法 |
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試料調製
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| 由来(天然) |
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| 緩衝液 | pH: 7.5 | ||||||||||||||||||||||||||||
| 試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||||||||||||
| 急速凍結 | 凍結剤: ETHANE |
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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: 300 kV / 照射モード: FLOOD BEAM |
| 電子レンズ | モード: DARK FIELD / 最大 デフォーカス(公称値): 2500 nm / 最小 デフォーカス(公称値): 1000 nm |
| 撮影 | 電子線照射量: 58 e/Å2 / フィルム・検出器のモデル: GATAN K3 (6k x 4k) |
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解析
| EMソフトウェア |
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| CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||
| 3次元再構成 | 解像度: 3.1 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 262752 / 対称性のタイプ: POINT |
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万見について





Homo sapiens (ヒト)
Encephalomyocarditis virus (脳心筋炎ウイルス)
米国, 5件
引用





PDBj



































FIELD EMISSION GUN