+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 7qi5 | ||||||||||||||||||
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タイトル | Human mitochondrial ribosome in complex with mRNA, A/A-, P/P- and E/E-tRNAs at 2.63 A resolution | ||||||||||||||||||
要素 |
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キーワード | RIBOSOME / mitochondrial translation / tRNA / mRNA / 2Fe-2S clusters / polyamines / rRNA modifications / post-translation modifications / cryo EM | ||||||||||||||||||
機能・相同性 | 機能・相同性情報 mitochondrial ribosome binding / rRNA import into mitochondrion / mitochondrial transcription / mitochondrial translational termination / mitochondrial translational elongation / mitochondrial ribosome assembly / translation release factor activity, codon nonspecific / positive regulation of mitochondrial translation / microprocessor complex / Mitochondrial translation elongation ...mitochondrial ribosome binding / rRNA import into mitochondrion / mitochondrial transcription / mitochondrial translational termination / mitochondrial translational elongation / mitochondrial ribosome assembly / translation release factor activity, codon nonspecific / positive regulation of mitochondrial translation / microprocessor complex / Mitochondrial translation elongation / Mitochondrial translation termination / Mitochondrial translation initiation / mitochondrial large ribosomal subunit / negative regulation of mitotic nuclear division / 加水分解酵素; エステル加水分解酵素; 5'-リン酸モノエステル産生エンドリボヌクレアーゼ / peptidyl-tRNA hydrolase / mitochondrial ribosome / mitochondrial small ribosomal subunit / mitochondrial translation / aminoacyl-tRNA hydrolase activity / positive regulation of proteolysis / ribosomal small subunit binding / anatomical structure morphogenesis / RNA processing / Mitochondrial protein degradation / rescue of stalled ribosome / apoptotic signaling pathway / cellular response to leukemia inhibitory factor / fibrillar center / double-stranded RNA binding / small ribosomal subunit rRNA binding / cell junction / regulation of translation / ribosomal small subunit assembly / small ribosomal subunit / 5S rRNA binding / large ribosomal subunit rRNA binding / nuclear membrane / endonuclease activity / cell population proliferation / tRNA binding / mitochondrial inner membrane / negative regulation of translation / nuclear body / rRNA binding / ribosome / structural constituent of ribosome / mitochondrial matrix / ribonucleoprotein complex / translation / protein domain specific binding / intracellular membrane-bounded organelle / mRNA binding / nucleotide binding / synapse / GTP binding / nucleolus / apoptotic process / positive regulation of DNA-templated transcription / mitochondrion / RNA binding / extracellular space / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | ||||||||||||||||||
生物種 | Homo sapiens (ヒト) | ||||||||||||||||||
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: 2.63 Å | ||||||||||||||||||
データ登録者 | Singh, V. / Itoh, Y. / Amunts, A. | ||||||||||||||||||
資金援助 | European Union, 5件
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引用 | ジャーナル: Nat Commun / 年: 2024 タイトル: Mitoribosome structure with cofactors and modifications reveals mechanism of ligand binding and interactions with L1 stalk. 著者: Vivek Singh / Yuzuru Itoh / Samuel Del'Olio / Asem Hassan / Andreas Naschberger / Rasmus Kock Flygaard / Yuko Nobe / Keiichi Izumikawa / Shintaro Aibara / Juni Andréll / Paul C Whitford / ...著者: Vivek Singh / Yuzuru Itoh / Samuel Del'Olio / Asem Hassan / Andreas Naschberger / Rasmus Kock Flygaard / Yuko Nobe / Keiichi Izumikawa / Shintaro Aibara / Juni Andréll / Paul C Whitford / Antoni Barrientos / Masato Taoka / Alexey Amunts / 要旨: The mitoribosome translates mitochondrial mRNAs and regulates energy conversion that is a signature of aerobic life forms. We present a 2.2 Å resolution structure of human mitoribosome together ...The mitoribosome translates mitochondrial mRNAs and regulates energy conversion that is a signature of aerobic life forms. We present a 2.2 Å resolution structure of human mitoribosome together with validated mitoribosomal RNA (rRNA) modifications, including aminoacylated CP-tRNA. The structure shows how mitoribosomal proteins stabilise binding of mRNA and tRNA helping to align it in the decoding center, whereas the GDP-bound mS29 stabilizes intersubunit communication. Comparison between different states, with respect to tRNA position, allowed us to characterize a non-canonical L1 stalk, and molecular dynamics simulations revealed how it facilitates tRNA transitions in a way that does not require interactions with rRNA. We also report functionally important polyamines that are depleted when cells are subjected to an antibiotic treatment. The structural, biochemical, and computational data illuminate the principal functional components of the translation mechanism in mitochondria and provide a description of the structure and function of the human mitoribosome. #1: ジャーナル: Nat Commun / 年: 2024 タイトル: Mitoribosome structure with cofactors and modifications reveals mechanism of ligand binding and interactions with L1 stalk. 著者: Vivek Singh / Yuzuru Itoh / Samuel Del'Olio / Asem Hassan / Andreas Naschberger / Rasmus Kock Flygaard / Yuko Nobe / Keiichi Izumikawa / Shintaro Aibara / Juni Andréll / Paul C Whitford / ...著者: Vivek Singh / Yuzuru Itoh / Samuel Del'Olio / Asem Hassan / Andreas Naschberger / Rasmus Kock Flygaard / Yuko Nobe / Keiichi Izumikawa / Shintaro Aibara / Juni Andréll / Paul C Whitford / Antoni Barrientos / Masato Taoka / Alexey Amunts / 要旨: The mitoribosome translates mitochondrial mRNAs and regulates energy conversion that is a signature of aerobic life forms. We present a 2.2 Å resolution structure of human mitoribosome together ...The mitoribosome translates mitochondrial mRNAs and regulates energy conversion that is a signature of aerobic life forms. We present a 2.2 Å resolution structure of human mitoribosome together with validated mitoribosomal RNA (rRNA) modifications, including aminoacylated CP-tRNA. The structure shows how mitoribosomal proteins stabilise binding of mRNA and tRNA helping to align it in the decoding center, whereas the GDP-bound mS29 stabilizes intersubunit communication. Comparison between different states, with respect to tRNA position, allowed us to characterize a non-canonical L1 stalk, and molecular dynamics simulations revealed how it facilitates tRNA transitions in a way that does not require interactions with rRNA. We also report functionally important polyamines that are depleted when cells are subjected to an antibiotic treatment. The structural, biochemical, and computational data illuminate the principal functional components of the translation mechanism in mitochondria and provide a description of the structure and function of the human mitoribosome. #2: ジャーナル: bioRxiv / 年: 2023 タイトル: Structure of mitoribosome reveals mechanism of mRNA binding, tRNA interactions with L1 stalk, roles of cofactors and rRNA modifications. 著者: Vivek Singh / Yuzuru Itoh / Samuel Del'Olio / Asem Hassan / Andreas Naschberger / Rasmus Kock Flygaard / Yuko Nobe / Keiichi Izumikawa / Shintaro Aibara / Juni Andréll / Paul C Whitford / ...著者: Vivek Singh / Yuzuru Itoh / Samuel Del'Olio / Asem Hassan / Andreas Naschberger / Rasmus Kock Flygaard / Yuko Nobe / Keiichi Izumikawa / Shintaro Aibara / Juni Andréll / Paul C Whitford / Antoni Barrientos / Masato Taoka / Alexey Amunts 要旨: The mitoribosome translates mitochondrial mRNAs and regulates energy conversion that is a signature of aerobic life forms. We present a 2.2 Å resolution structure of human mitoribosome together with ...The mitoribosome translates mitochondrial mRNAs and regulates energy conversion that is a signature of aerobic life forms. We present a 2.2 Å resolution structure of human mitoribosome together with validated mitoribosomal RNA (rRNA) modifications, including aminoacylated CP-tRNA . The structure shows how mitoribosomal proteins stabilise binding of mRNA and tRNA helping to align it in the decoding center, whereas the GDP-bound mS29 stabilizes intersubunit communication. Comparison between different states, with respect to tRNA position, allowed to characterize a non-canonical L1 stalk, and molecular dynamics simulations revealed how it facilitates tRNA transition in a way that does not require interactions with rRNA. We also report functionally important polyamines that are depleted when cells are subjected to an antibiotic treatment. The structural, biochemical, and computational data illuminate the principal functional components of the translation mechanism in mitochondria and provide the most complete description so far of the structure and function of the human mitoribosome. | ||||||||||||||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 7qi5.cif.gz | 7.1 MB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb7qi5.ent.gz | 表示 | PDB形式 | |
PDBx/mmJSON形式 | 7qi5.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 | 7qi5_validation.pdf.gz | 2.5 MB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 7qi5_full_validation.pdf.gz | 2.6 MB | 表示 | |
XML形式データ | 7qi5_validation.xml.gz | 371.2 KB | 表示 | |
CIF形式データ | 7qi5_validation.cif.gz | 663.2 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/qi/7qi5 ftp://data.pdbj.org/pub/pdb/validation_reports/qi/7qi5 | HTTPS FTP |
-関連構造データ
関連構造データ | 13981MC 7qi4C 7qi6C 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 (文献) |
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類似構造データ | 類似検索 - 機能・相同性F&H 検索 |
-リンク
-集合体
登録構造単位 |
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1 |
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-要素
-RNA鎖 , 7種, 7分子 AAAwAxAyAzAB
#1: RNA鎖 | 分子量: 306218.312 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: GenBank: 1858624182 |
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#32: RNA鎖 | 分子量: 21627.838 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: GenBank: 1896813690 |
#33: RNA鎖 | 分子量: 22354.291 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) |
#34: RNA鎖 | 分子量: 22369.307 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) |
#35: RNA鎖 | 分子量: 10826.415 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) |
#36: RNA鎖 | 分子量: 500727.125 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: GenBank: 208964619 |
#37: RNA鎖 | 分子量: 22989.752 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: GenBank: NC_012920.1 |
+28S ribosomal protein ... , 26種, 26分子 ABACADAEAFAGAHAIAJAKALAMANAOAPARASATAUAVAWAXAYAZA0A1
-タンパク質 , 8種, 8分子 AQA2A3A4bopq
#17: タンパク質 | 分子量: 10806.689 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: A0A2J8VEN6 |
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#29: タンパク質 | 分子量: 13540.856 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: Q96BP2 |
#30: タンパク質 | 分子量: 22395.326 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: Q9NWT8 |
#31: タンパク質 | 分子量: 78648.547 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: Q96EY7 |
#70: タンパク質 | 分子量: 23352.633 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: Q8N983 |
#82: タンパク質 | 分子量: 12292.333 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: Q9BQC6 |
#83: タンパク質 | 分子量: 23674.203 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: Q14197, peptidyl-tRNA hydrolase |
#84: タンパク質 | 分子量: 25426.895 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: cell / 由来: (天然) Homo sapiens (ヒト) / 参照: UniProt: Q8TAE8 |
+39S ribosomal protein ... , 48種, 53分子 DEFIJKLMNOPQRSTUVWXYZ012345678...
-非ポリマー , 12種, 7991分子
#90: 化合物 | ChemComp-NAD / | ||||||||||||||||||
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#91: 化合物 | ChemComp-SPM / | ||||||||||||||||||
#92: 化合物 | ChemComp-SPD / #93: 化合物 | ChemComp-MG / #94: 化合物 | ChemComp-K / #95: 化合物 | #96: 化合物 | #97: 化合物 | ChemComp-ATP / | #98: 化合物 | ChemComp-GDP / | #99: 化合物 | ChemComp-PUT / | #100: 化合物 | ChemComp-VAL / | #101: 水 | ChemComp-HOH / | |
-詳細
研究の焦点であるリガンドがあるか | 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 |
-試料調製
構成要素 | 名称: Human mitochondrial ribosome / タイプ: RIBOSOME / Entity ID: #1-#69, #71-#89 / 由来: NATURAL |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
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 |
-電子顕微鏡撮影
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI TITAN KRIOS |
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 / 最大 デフォーカス(公称値): 2800 nm / 最小 デフォーカス(公称値): 600 nm |
撮影 | 電子線照射量: 30 e/Å2 / 検出モード: COUNTING フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
電子光学装置 | エネルギーフィルタースリット幅: 20 eV |
-解析
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3次元再構成 | 解像度: 2.63 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 82522 / 対称性のタイプ: POINT |