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基本情報
登録情報 | データベース: PDB / ID: 7nk9 | |||||||||
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タイトル | Mycobacterium smegmatis ATP synthase Fo domain state 1 | |||||||||
![]() | (ATP synthase ...![]() | |||||||||
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機能・相同性 | ![]() proton motive force-driven plasma membrane ATP synthesis / proton-transporting ATP synthase complex, coupling factor F(o) / proton-transporting ATP synthase complex, catalytic core F(1) / proton-transporting ATPase activity, rotational mechanism / proton-transporting ATP synthase activity, rotational mechanism / ![]() ![]() ![]() ![]() 類似検索 - 分子機能 | |||||||||
生物種 | ![]() ![]() ![]() ![]() | |||||||||
手法 | ![]() ![]() ![]() | |||||||||
![]() | Montgomery, M.G. / Petri, J. / Spikes, T.E. / Walker, J.E. | |||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structure of the ATP synthase from provides targets for treating tuberculosis. 著者: Martin G Montgomery / Jessica Petri / Tobias E Spikes / John E Walker / ![]() 要旨: The structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from This analysis confirms features in a prior description of the structure of the enzyme, ...The structure has been determined by electron cryomicroscopy of the adenosine triphosphate (ATP) synthase from This analysis confirms features in a prior description of the structure of the enzyme, but it also describes other highly significant attributes not recognized before that are crucial for understanding the mechanism and regulation of the mycobacterial enzyme. First, we resolved not only the three main states in the catalytic cycle described before but also eight substates that portray structural and mechanistic changes occurring during a 360° catalytic cycle. Second, a mechanism of auto-inhibition of ATP hydrolysis involves not only the engagement of the C-terminal region of an α-subunit in a loop in the γ-subunit, as proposed before, but also a "fail-safe" mechanism involving the b'-subunit in the peripheral stalk that enhances engagement. A third unreported characteristic is that the fused bδ-subunit contains a duplicated domain in its N-terminal region where the two copies of the domain participate in similar modes of attachment of the two of three N-terminal regions of the α-subunits. The auto-inhibitory plus the associated "fail-safe" mechanisms and the modes of attachment of the α-subunits provide targets for development of innovative antitubercular drugs. The structure also provides support for an observation made in the bovine ATP synthase that the transmembrane proton-motive force that provides the energy to drive the rotary mechanism is delivered directly and tangentially to the rotor via a Grotthuss water chain in a polar L-shaped tunnel. | |||||||||
履歴 |
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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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PDBx/mmCIF形式 | ![]() | 386.1 KB | 表示 | ![]() |
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PDB形式 | ![]() | 324.5 KB | 表示 | ![]() |
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アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
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-関連構造データ
関連構造データ | ![]() 12434MC ![]() 7njkC ![]() 7njlC ![]() 7njmC ![]() 7njnC ![]() 7njoC ![]() 7njpC ![]() 7njqC ![]() 7njrC ![]() 7njsC ![]() 7njtC ![]() 7njuC ![]() 7njvC ![]() 7njwC ![]() 7njxC ![]() 7njyC ![]() 7nk7C ![]() 7nkbC ![]() 7nkdC ![]() 7nkhC ![]() 7nkjC ![]() 7nkkC ![]() 7nklC ![]() 7nknC ![]() 7nkpC ![]() 7nkqC ![]() 7nl9C C: 同じ文献を引用 ( M: このデータのモデリングに利用したマップデータ |
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類似構造データ |
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集合体
登録構造単位 | ![]()
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要素
-ATP synthase ... , 6種, 14分子 GHLMNOPQRSTabd
#1: タンパク質 | 分子量: 33439.836 Da / 分子数: 1 / 由来タイプ: 組換発現 詳細: This alignment is incorrect. The initial 13 residues in the model should align with residues 53-65. 由来: (組換発現) ![]() 株: ATCC 700084 / mc(2)155 / 遺伝子: atpG, MSMEG_4937, MSMEI_4810 / 発現宿主: ![]() ![]() | ||||||
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#2: タンパク質 | 分子量: 13277.741 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) ![]() 株: ATCC 700084 / mc(2)155 / 遺伝子: atpC, MSMEG_4935, MSMEI_4808 / 発現宿主: ![]() ![]() | ||||||
#3: タンパク質 | ![]() 分子量: 8597.982 Da / 分子数: 9 / 由来タイプ: 組換発現 / 詳細: Uniprot A0R205. The crossref box is missing below. 由来: (組換発現) ![]() 株: ATCC 700084 / mc(2)155 / 遺伝子: atpE, MSMEG_4941 / 発現宿主: ![]() ![]() #4: タンパク質 | | ![]() 分子量: 27568.482 Da / 分子数: 1 / 由来タイプ: 組換発現 / 詳細: A0R206. The crossref box is missing below. 由来: (組換発現) ![]() 株: ATCC 700084 / mc(2)155 / 遺伝子: atpB, MSMEG_4942 / 発現宿主: ![]() ![]() #5: タンパク質 | | ![]() 分子量: 19018.170 Da / 分子数: 1 / 由来タイプ: 組換発現 / 詳細: uniprot A0R204. The crossref box is missing below. 由来: (組換発現) ![]() 株: ATCC 700084 / mc(2)155 / 遺伝子: atpF, MSMEG_4940, MSMEI_4813 / 発現宿主: ![]() ![]() #6: タンパク質 | | ![]() 分子量: 47504.723 Da / 分子数: 1 / 由来タイプ: 組換発現 / 詳細: uniprot A0R203. The crossref box is missing. 由来: (組換発現) ![]() 株: ATCC 700084 / mc(2)155 / 遺伝子: atpFH, atpF, atpH, MSMEG_4939, MSMEI_4812 / 発現宿主: ![]() ![]() |
-実験情報
-実験
実験 | 手法: ![]() |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: ![]() |
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試料調製
構成要素 | 名称: Mycobacterium smegmatis ATP synthase / タイプ: COMPLEX / Entity ID: all / 由来: RECOMBINANT |
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分子量 | 実験値: YES |
由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() ![]() |
緩衝液 | pH: 8 |
試料 | 包埋: NO / シャドウイング: NO / 染色![]() ![]() |
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: FEI TITAN KRIOS |
電子銃 | 電子線源![]() ![]() |
電子レンズ | モード: BRIGHT FIELD![]() |
撮影 | 電子線照射量: 59.86 e/Å2 / フィルム・検出器のモデル: GATAN K3 (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: 2.9 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 127186 / 対称性のタイプ: POINT |