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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: 9eih | |||||||||||||||||||||||||||
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タイトル | Import stalled PINK1 TOM complex | |||||||||||||||||||||||||||
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![]() | TRANSLOCASE / PINK1 / TOM complex / VDAC | |||||||||||||||||||||||||||
機能・相同性 | ![]() positive regulation of synaptic transmission, dopaminergic / positive regulation of free ubiquitin chain polymerization / positive regulation of cristae formation / tRNA import into mitochondrion / TOM complex / mitochondrial transmembrane transport / voltage-gated monoatomic anion channel activity / mitochondrial outer membrane permeabilization / regulation of protein targeting to mitochondrion / mitochondrion to lysosome vesicle-mediated transport ...positive regulation of synaptic transmission, dopaminergic / positive regulation of free ubiquitin chain polymerization / positive regulation of cristae formation / tRNA import into mitochondrion / TOM complex / mitochondrial transmembrane transport / voltage-gated monoatomic anion channel activity / mitochondrial outer membrane permeabilization / regulation of protein targeting to mitochondrion / mitochondrion to lysosome vesicle-mediated transport / Mitochondrial calcium ion transport / maintenance of protein location in mitochondrion / mitochondrion targeting sequence binding / establishment of protein localization to mitochondrion / protein kinase B binding / mitochondrial outer membrane translocase complex / cellular response to hydrogen sulfide / Lewy body / negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway / TORC2 signaling / regulation of autophagy of mitochondrion / phospholipid scramblase activity / regulation of synaptic vesicle transport / protein insertion into mitochondrial outer membrane / ceramide binding / positive regulation of mitochondrial electron transport, NADH to ubiquinone / mitochondria-associated endoplasmic reticulum membrane contact site / regulation of hydrogen peroxide metabolic process / migrasome / regulation of oxidative phosphorylation / negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway / C3HC4-type RING finger domain binding / regulation of cellular response to oxidative stress / dopamine secretion / protein-transporting ATPase activity / voltage-gated monoatomic ion channel activity / positive regulation of dopamine secretion / negative regulation of autophagosome assembly / binding of sperm to zona pellucida / autophagy of mitochondrion / phosphatidylcholine binding / positive regulation of type 2 mitophagy / oxysterol binding / Mitochondrial protein import / cellular response to toxic substance / negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway / regulation of mitochondrion organization / monoatomic anion transport / negative regulation of JNK cascade / positive regulation of ubiquitin-protein transferase activity / protein targeting to mitochondrion / positive regulation of protein targeting to mitochondrion / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / regulation of reactive oxygen species metabolic process / peptidase activator activity / phospholipid translocation / cholesterol binding / negative regulation of macroautophagy / astrocyte projection / positive regulation of mitochondrial fission / porin activity / negative regulation of mitophagy / pore complex / FOXO-mediated transcription of cell death genes / negative regulation of intrinsic apoptotic signaling pathway / protein import into mitochondrial matrix / positive regulation of release of cytochrome c from mitochondria / positive regulation of ATP biosynthetic process / hemopoiesis / negative regulation of reactive oxygen species metabolic process / mitochondrial nucleoid / positive regulation of macroautophagy / protein transmembrane transporter activity / regulation of protein ubiquitination / regulation of proteasomal protein catabolic process / negative regulation of mitochondrial fission / regulation of protein-containing complex assembly / mitophagy / monoatomic ion transport / sperm midpiece / positive regulation of protein ubiquitination / regulation of mitochondrial membrane potential / PINK1-PRKN Mediated Mitophagy / acrosomal vesicle / positive regulation of translation / response to ischemia / cell periphery / respiratory electron transport chain / mitochondrion organization / macroautophagy / mitochondrial membrane / regulation of protein stability / mitochondrial intermembrane space / kinase binding / kinase activity / unfolded protein binding / growth cone / cell body / cellular response to oxidative stress / response to oxidative stress 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: 3.1 Å | |||||||||||||||||||||||||||
![]() | Kirk, N.S. / Glukhova, A. / Callegari, S. / Komander, D. | |||||||||||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structure of human PINK1 at a mitochondrial TOM-VDAC array. 著者: Sylvie Callegari / Nicholas S Kirk / Zhong Yan Gan / Toby Dite / Simon A Cobbold / Andrew Leis / Laura F Dagley / Alisa Glukhova / David Komander / ![]() 要旨: Mutations in the ubiquitin kinase PINK1 cause early-onset Parkinson's disease, but how PINK1 is stabilized at depolarized mitochondrial translocase complexes has remained poorly understood. We ...Mutations in the ubiquitin kinase PINK1 cause early-onset Parkinson's disease, but how PINK1 is stabilized at depolarized mitochondrial translocase complexes has remained poorly understood. We determined a 3.1-angstrom resolution cryo-electron microscopy structure of dimeric human PINK1 stabilized at an endogenous array of mitochondrial translocase of the outer membrane (TOM) and voltage-dependent anion channel (VDAC) complexes. Symmetric arrangement of two TOM core complexes around a central VDAC2 dimer is facilitated by TOM5 and TOM20, both of which also bind PINK1 kinase C-lobes. PINK1 enters mitochondria through the proximal TOM40 barrel of the TOM core complex, guided by TOM7 and TOM22. Our structure explains how human PINK1 is stabilized at the TOM complex and regulated by oxidation, uncovers a previously unknown TOM-VDAC assembly, and reveals how a physiological substrate traverses TOM40 during translocation. | |||||||||||||||||||||||||||
履歴 |
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構造の表示
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 | ![]() | 713.3 KB | 表示 | ![]() |
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PDB形式 | ![]() | 583.6 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 2 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 2 MB | 表示 | |
XML形式データ | ![]() | 112.5 KB | 表示 | |
CIF形式データ | ![]() | 170.3 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 48083MC ![]() 9eiiC ![]() 9eijC 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 ![]() |
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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
-Mitochondrial import receptor subunit ... , 6種, 22分子 CDGHIJKLYZMNWXOPUVQRST
#1: タンパク質 | 分子量: 16319.862 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() #3: タンパク質 | 分子量: 37926.926 Da / 分子数: 4 / 由来タイプ: 天然 / 由来: (天然) ![]() #4: タンパク質 | 分子量: 6045.318 Da / 分子数: 4 / 由来タイプ: 天然 / 由来: (天然) ![]() #5: タンパク質 | 分子量: 6256.473 Da / 分子数: 4 / 由来タイプ: 天然 / 由来: (天然) ![]() #6: タンパク質 | 分子量: 8007.988 Da / 分子数: 4 / 由来タイプ: 天然 / 由来: (天然) ![]() #7: タンパク質 | 分子量: 15532.528 Da / 分子数: 4 / 由来タイプ: 天然 / 由来: (天然) ![]() |
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-タンパク質 , 2種, 4分子 EFAB
#2: タンパク質 | 分子量: 31600.445 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() #8: タンパク質 | 分子量: 65561.562 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() 参照: UniProt: Q9BXM7, non-specific serine/threonine protein kinase |
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-非ポリマー , 1種, 17分子 
#9: 化合物 | ChemComp-PC1 / |
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-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: 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: Import stalled PINK1 TOM complex / タイプ: COMPLEX / Entity ID: #8, #1-#7 / 由来: RECOMBINANT |
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分子量 | 値: 0.75 MDa / 実験値: NO |
由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() |
緩衝液 | pH: 7.4 |
試料 | 濃度: 4 mg/ml / 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: Titan Krios / 画像提供: FEI Company |
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顕微鏡 | モデル: TFS KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2000 nm / 最小 デフォーカス(公称値): 500 nm / Cs: 2.7 mm / C2レンズ絞り径: 50 µm |
撮影 | 電子線照射量: 52.4 e/Å2 フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) |
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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: 3.1 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 347000 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
精密化 | 最高解像度: 3.1 Å 立体化学のターゲット値: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
拘束条件 |
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