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基本情報
登録情報 | ![]() | |||||||||||||||
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タイトル | Human ATP synthase state 2 (combined) | |||||||||||||||
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![]() | MEMBRANE PROTEIN | |||||||||||||||
機能・相同性 | ![]() negative regulation of cell adhesion involved in substrate-bound cell migration / Formation of ATP by chemiosmotic coupling / Cristae formation / ATP biosynthetic process / angiostatin binding / Mitochondrial protein import / mitochondrial proton-transporting ATP synthase complex assembly / proton-transporting ATP synthase complex / oxidative phosphorylation / cellular response to interleukin-7 ...negative regulation of cell adhesion involved in substrate-bound cell migration / Formation of ATP by chemiosmotic coupling / Cristae formation / ATP biosynthetic process / angiostatin binding / Mitochondrial protein import / mitochondrial proton-transporting ATP synthase complex assembly / proton-transporting ATP synthase complex / oxidative phosphorylation / cellular response to interleukin-7 / response to copper ion / response to muscle activity / cellular response to nitric oxide / : / : / : / : / proton-transporting ATP synthase complex, coupling factor F(o) / mitochondrial nucleoid / : / MHC class I protein binding / negative regulation of endothelial cell proliferation / proton transmembrane transporter activity / proton motive force-driven ATP synthesis / positive regulation of blood vessel endothelial cell migration / response to hyperoxia / generation of precursor metabolites and energy / proton-transporting ATP synthase complex, catalytic core F(1) / cellular response to dexamethasone stimulus / H+-transporting two-sector ATPase / substantia nigra development / proton-transporting ATPase activity, rotational mechanism / proton transmembrane transport / proton-transporting ATP synthase activity, rotational mechanism / proton motive force-driven mitochondrial ATP synthesis / Mitochondrial protein degradation / lipid metabolic process / regulation of intracellular pH / Transcriptional activation of mitochondrial biogenesis / mitochondrial membrane / aerobic respiration / ADP binding / osteoblast differentiation / nuclear membrane / protease binding / angiogenesis / response to ethanol / mitochondrial inner membrane / mitochondrial matrix / hydrolase activity / membrane raft / lipid binding / cell surface / ATP hydrolysis activity / mitochondrion / RNA binding / extracellular exosome / ATP binding / membrane / nucleus / plasma membrane 類似検索 - 分子機能 | |||||||||||||||
生物種 | ![]() | |||||||||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 2.77 Å | |||||||||||||||
![]() | Lai Y / Zhang Y / Liu F / Gao Y / Gong H / Rao Z | |||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structure of the human ATP synthase. 著者: Yuezheng Lai / Yuying Zhang / Shan Zhou / Jinxu Xu / Zhanqiang Du / Ziyan Feng / Long Yu / Ziqing Zhao / Weiwei Wang / Yanting Tang / Xiuna Yang / Luke W Guddat / Fengjiang Liu / Yan Gao / ...著者: Yuezheng Lai / Yuying Zhang / Shan Zhou / Jinxu Xu / Zhanqiang Du / Ziyan Feng / Long Yu / Ziqing Zhao / Weiwei Wang / Yanting Tang / Xiuna Yang / Luke W Guddat / Fengjiang Liu / Yan Gao / Zihe Rao / Hongri Gong / ![]() ![]() 要旨: Biological energy currency ATP is produced by FF-ATP synthase. However, the molecular mechanism for human ATP synthase action remains unknown. Here, we present snapshot images for three main ...Biological energy currency ATP is produced by FF-ATP synthase. However, the molecular mechanism for human ATP synthase action remains unknown. Here, we present snapshot images for three main rotational states and one substate of human ATP synthase using cryoelectron microscopy. These structures reveal that the release of ADP occurs when the β subunit of FF-ATP synthase is in the open conformation, showing how ADP binding is coordinated during synthesis. The accommodation of the symmetry mismatch between F and F motors is resolved by the torsional flexing of the entire complex, especially the γ subunit, and the rotational substep of the c subunit. Water molecules are identified in the inlet and outlet half-channels, suggesting that the proton transfer in these two half-channels proceed via a Grotthus mechanism. Clinically relevant mutations are mapped to the structure, showing that they are mainly located at the subunit-subunit interfaces, thus causing instability of the complex. | |||||||||||||||
履歴 |
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構造の表示
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ダウンロードとリンク
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マップデータ | ![]() | 473.7 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 27.2 KB 27.2 KB | 表示 表示 | ![]() |
画像 | ![]() | 130.1 KB | ||
Filedesc metadata | ![]() | 7.8 KB | ||
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 | ![]() 8h9tMC ![]() 8h9eC ![]() 8h9fC ![]() 8h9gC ![]() 8h9iC ![]() 8h9jC ![]() 8h9kC ![]() 8h9lC ![]() 8h9mC ![]() 8h9nC ![]() 8h9pC ![]() 8h9qC ![]() 8h9rC ![]() 8h9sC ![]() 8h9uC ![]() 8h9vC C: 同じ文献を引用 ( M: このマップから作成された原子モデル |
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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
EMDBのページ | ![]() ![]() |
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「今月の分子」の関連する項目 |
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マップ
ファイル | ![]() | ||||||||||||||||||||
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ボクセルのサイズ | X=Y=Z: 0.73 Å | ||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
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試料の構成要素
+全体 : Human ATP synthase
+超分子 #1: Human ATP synthase
+分子 #1: ATP synthase F(0) complex subunit B1, mitochondrial
+分子 #2: ATP synthase-coupling factor 6, mitochondrial
+分子 #3: ATP synthase subunit d, mitochondrial
+分子 #4: ATP synthase F(0) complex subunit C1, mitochondrial
+分子 #5: ATP synthase subunit delta, mitochondrial
+分子 #6: ATP synthase subunit epsilon, mitochondrial
+分子 #7: ATP synthase subunit a
+分子 #8: ATP synthase subunit ATP5MJ, mitochondrial
+分子 #9: ATP synthase subunit f, mitochondrial
+分子 #10: ATP synthase subunit g, mitochondrial
+分子 #11: ATP synthase subunit e, mitochondrial
+分子 #12: ATP synthase protein 8
+分子 #13: ATP synthase subunit alpha, mitochondrial
+分子 #14: ATP synthase subunit beta, mitochondrial
+分子 #15: ATP synthase subunit gamma, mitochondrial
+分子 #16: ATP synthase subunit O, mitochondrial
+分子 #17: ADENOSINE-5'-TRIPHOSPHATE
+分子 #18: MAGNESIUM ION
+分子 #19: ADENOSINE-5'-DIPHOSPHATE
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.4 |
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グリッド | モデル: Quantifoil R1.2/1.3 / 支持フィルム - 材質: CARBON / 支持フィルム - トポロジー: HOLEY |
凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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特殊光学系 | エネルギーフィルター - 名称: TFS Selectris X / エネルギーフィルター - スリット幅: 10 eV |
撮影 | フィルム・検出器のモデル: FEI FALCON IV (4k x 4k) 平均電子線量: 50.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2.4 µm / 最小 デフォーカス(公称値): 1.2 µm |
試料ステージ | ホルダー冷却材: NITROGEN |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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画像解析
初期モデル | モデルのタイプ: OTHER / 詳細: AlphaFold |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 2.77 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 37480 |
初期 角度割当 | タイプ: MAXIMUM LIKELIHOOD / ソフトウェア - 名称: cryoSPARC |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD / ソフトウェア - 名称: cryoSPARC |