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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: 5aj4 | |||||||||
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タイトル | Structure of the 55S mammalian mitoribosome. | |||||||||
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![]() | RIBOSOME / TRANSLATION / MITOCHONDRIA / MAMMALIAN 55S MITORIBOSOME / MAMMALIAN 55S MITOCHONDRIAL RIBOSOME / 28S SMALL SUBUNIT / 39S LARGE SUBUNIT / MRNA / TRNA / PTC / DECODING CENTER / CRYO- EM / SINGLE PARTICLE ANALYSIS | |||||||||
機能・相同性 | ![]() Mitochondrial translation elongation / Mitochondrial translation termination / rRNA import into mitochondrion / mitochondrial translational termination / mitochondrial ribosome assembly / mitochondrial translational elongation / ribonuclease III activity / translation release factor activity, codon nonspecific / Mitochondrial protein degradation / mitochondrial large ribosomal subunit ...Mitochondrial translation elongation / Mitochondrial translation termination / rRNA import into mitochondrion / mitochondrial translational termination / mitochondrial ribosome assembly / mitochondrial translational elongation / ribonuclease III activity / translation release factor activity, codon nonspecific / Mitochondrial protein degradation / mitochondrial large ribosomal subunit / peptidyl-tRNA hydrolase / mitochondrial ribosome / mitochondrial small ribosomal subunit / peptidyl-tRNA hydrolase activity / mitochondrial translation / organelle membrane / ribosomal small subunit binding / RNA processing / cell junction / regulation of translation / large ribosomal subunit / double-stranded RNA binding / small ribosomal subunit / 5S rRNA binding / rRNA binding / nuclear body / ribosome / structural constituent of ribosome / protein domain specific binding / translation / ribonucleoprotein complex / intracellular membrane-bounded organelle / mitochondrion / RNA binding / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
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: 3.8 Å | |||||||||
![]() | Greber, B.J. / Bieri, P. / Leibundgut, M. / Leitner, A. / Aebersold, R. / Boehringer, D. / Ban, N. | |||||||||
![]() | ![]() タイトル: Ribosome. The complete structure of the 55S mammalian mitochondrial ribosome. 著者: Basil J Greber / Philipp Bieri / Marc Leibundgut / Alexander Leitner / Ruedi Aebersold / Daniel Boehringer / Nenad Ban / ![]() 要旨: Mammalian mitochondrial ribosomes (mitoribosomes) synthesize mitochondrially encoded membrane proteins that are critical for mitochondrial function. Here we present the complete atomic structure of ...Mammalian mitochondrial ribosomes (mitoribosomes) synthesize mitochondrially encoded membrane proteins that are critical for mitochondrial function. Here we present the complete atomic structure of the porcine 55S mitoribosome at 3.8 angstrom resolution by cryo-electron microscopy and chemical cross-linking/mass spectrometry. The structure of the 28S subunit in the complex was resolved at 3.6 angstrom resolution by focused alignment, which allowed building of a detailed atomic structure including all of its 15 mitoribosomal-specific proteins. The structure reveals the intersubunit contacts in the 55S mitoribosome, the molecular architecture of the mitoribosomal messenger RNA (mRNA) binding channel and its interaction with transfer RNAs, and provides insight into the highly specialized mechanism of mRNA recruitment to the 28S subunit. Furthermore, the structure contributes to a mechanistic understanding of aminoglycoside ototoxicity. | |||||||||
履歴 |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "LA" IN EACH CHAIN ON SHEET RECORDS BELOW ...SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "LA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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構造の表示
ムービー |
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構造ビューア | 分子: ![]() ![]() |
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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 | ![]() | 3.8 MB | 表示 | ![]() |
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PDB形式 | ![]() | 表示 | ![]() | |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-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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1 |
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要素
+MITORIBOSOMAL ... , 82種, 82分子 AAABACAEAFAGAIAJAKALANAOAPAQARAUAaAbAcAdAeAfAgAhAiAjAkAmAnAo...
-RNA鎖 , 2種, 3分子 AVAYAX
#17: RNA鎖 | 分子量: 19163.691 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() #18: RNA鎖 | | 分子量: 3545.419 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() |
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-タンパク質 , 2種, 2分子 ApBz
#33: タンパク質 | 分子量: 22027.184 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() |
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#88: タンパク質 | 分子量: 8017.875 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: BUILT AS UNK / 由来: (天然) ![]() ![]() |
-タンパク質・ペプチド , 2種, 2分子 AsAz
#34: タンパク質・ペプチド | 分子量: 1379.692 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() |
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#35: タンパク質・ペプチド | 分子量: 1464.797 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() ![]() |
-非ポリマー , 4種, 698分子 






#89: 化合物 | ChemComp-MG / #90: 化合物 | ChemComp-ZN / #91: 化合物 | ChemComp-GDP / | #92: 水 | ChemComp-HOH / | |
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-詳細
Has protein modification | Y |
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配列の詳細 | RESIDUES 251-266 OF US9M BUILT AS UNK RESIDUES 309-356 OF MS22 BUILT AS UNK PPR FOLD OF mS27 BUILT ...RESIDUES 251-266 OF US9M BUILT AS UNK RESIDUES 309-356 OF MS22 BUILT AS UNK PPR FOLD OF mS27 BUILT AS UNK RESIDUES 52-69 OF MS29 BUILT AS UNK RESIDUES 152-158 OF MS34 BUILT AS UNK N-TERMINAL SEQUENCE OF MS38 IS MISSING PPR FOLD OF MS39 BUILT AS UNK ALL RESIDUES OF CHAINS s,z (UNASSIGNED |
-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: SUS SCROFA 55S MITOCHONDRIAL RIBOSOME / タイプ: RIBOSOME 詳細: QUANTIFOIL HOLEY CARBON GRIDS WERE COATED WITH A THIN CARBON FILM. |
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緩衝液 | 名称: 20 MM HEPES-KOH, 50 MM KCL, 40 MM MGCL2, 1 MM DTT / pH: 7.4 / 詳細: 20 MM HEPES-KOH, 50 MM KCL, 40 MM MGCL2, 1 MM DTT |
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: CARBON |
急速凍結 | 装置: HOMEMADE PLUNGER / 凍結剤: ETHANE-PROPANE / 詳細: MIXTURE OF LIQUID ETHANE AND PROPANE |
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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 / 日付: 2014年5月30日 詳細: IMAGES WERE ACQUIRED IN 2 SESSIONS ON A FEI TITAN KRIOS IN MAY 2014. |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 59000 X / 倍率(補正後): 100000 X / 最大 デフォーカス(公称値): 3000 nm / 最小 デフォーカス(公称値): 800 nm / Cs: 2.7 mm |
試料ホルダ | 温度: 85 K |
撮影 | 電子線照射量: 20 e/Å2 フィルム・検出器のモデル: FEI FALCON II (4k x 4k) |
放射波長 | 相対比: 1 |
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解析
EMソフトウェア |
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CTF補正 | 詳細: PER DETECTOR FRAME | ||||||||||||||||||||||||
対称性 | 点対称性: C1 (非対称) | ||||||||||||||||||||||||
3次元再構成 | 手法: MAXIMUM LIKELIHOOD BASED REFINEMENT IMPLEMENTED IN RELION. 解像度: 3.8 Å / 粒子像の数: 60872 / ピクセルサイズ(実測値): 1.39 Å 詳細: FOR VISUALIZATION PURPOSES THE FINAL MAP WAS FILTERED AND AMPLITUDE CORRECTED IN RELION. THE COMBINED COORDINATES WERE REFINED IN RECIPROCAL SPACE USING PHENIX.REFINE AGAINST THE MLHL TARGET. ...詳細: FOR VISUALIZATION PURPOSES THE FINAL MAP WAS FILTERED AND AMPLITUDE CORRECTED IN RELION. THE COMBINED COORDINATES WERE REFINED IN RECIPROCAL SPACE USING PHENIX.REFINE AGAINST THE MLHL TARGET. FOR THIS, THE CRYO-EM MAPS (EMD-2914) WERE CONVERTED TO RECIPROCAL SPACE STRUCTURE FACTORS. 対称性のタイプ: POINT | ||||||||||||||||||||||||
原子モデル構築 | プロトコル: OTHER / 空間: REAL / 詳細: REFINEMENT PROTOCOL--HIGH RESOLUTION CRYO-EM | ||||||||||||||||||||||||
精密化 | 最高解像度: 3.8 Å | ||||||||||||||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 3.8 Å
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