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基本情報
登録情報 | ![]() | ||||||||||||
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タイトル | 21bin20S complex (NSF-alphaSNAP-2:1 syntaxin-1a:SNAP-25), non-hydrolyzing, class 11 | ||||||||||||
![]() | Sharpened map from CryoSPARC NU-Refine, B = 121.7 | ||||||||||||
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![]() | ATPase / SNARE / hydrolysis / disassembly / translocation / exocytosis / neurotransmitter release / synapse / synaptic transmission / membrane fusion / HYDROLASE | ||||||||||||
機能・相同性 | ![]() Intra-Golgi traffic / Retrograde transport at the Trans-Golgi-Network / COPI-dependent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / soluble NSF attachment protein activity / BLOC-1 complex / myosin head/neck binding / synaptic vesicle fusion to presynaptic active zone membrane / Other interleukin signaling / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex ...Intra-Golgi traffic / Retrograde transport at the Trans-Golgi-Network / COPI-dependent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / soluble NSF attachment protein activity / BLOC-1 complex / myosin head/neck binding / synaptic vesicle fusion to presynaptic active zone membrane / Other interleukin signaling / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex / synaptobrevin 2-SNAP-25-syntaxin-1a complex / presynaptic dense core vesicle exocytosis / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex / extrinsic component of presynaptic membrane / calcium ion-regulated exocytosis of neurotransmitter / Glutamate Neurotransmitter Release Cycle / Norepinephrine Neurotransmitter Release Cycle / Acetylcholine Neurotransmitter Release Cycle / Serotonin Neurotransmitter Release Cycle / COPII-mediated vesicle transport / GABA synthesis, release, reuptake and degradation / positive regulation of norepinephrine secretion / positive regulation of catecholamine secretion / regulated exocytosis / Dopamine Neurotransmitter Release Cycle / synaptic vesicle docking / SNARE complex disassembly / Golgi Associated Vesicle Biogenesis / regulation of synaptic vesicle priming / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / protein-containing complex disassembly / regulation of establishment of protein localization / positive regulation of calcium ion-dependent exocytosis / ribbon synapse / vesicle docking / regulation of exocytosis / secretion by cell / chloride channel inhibitor activity / SNAP receptor activity / SNARE complex / calcium-ion regulated exocytosis / vesicle fusion / actomyosin / ATP-dependent protein disaggregase activity / hormone secretion / LGI-ADAM interactions / positive regulation of ATP-dependent activity / positive regulation of hormone secretion / intra-Golgi vesicle-mediated transport / Golgi to plasma membrane protein transport / ATP-dependent protein binding / Golgi stack / neurotransmitter secretion / protein localization to membrane / apical protein localization / syntaxin binding / vesicle-fusing ATPase / insulin secretion / syntaxin-1 binding / endosomal transport / Neutrophil degranulation / SNARE complex assembly / positive regulation of neurotransmitter secretion / neurotransmitter transport / regulation of synapse assembly / synaptic vesicle priming / myosin binding / response to gravity / regulation of neuron projection development / positive regulation of receptor recycling / exocytosis / associative learning / modulation of excitatory postsynaptic potential / positive regulation of exocytosis / synaptic vesicle exocytosis / protein sumoylation / synaptic vesicle endocytosis / voltage-gated potassium channel activity / positive regulation of excitatory postsynaptic potential / long-term memory / axonal growth cone / calcium channel inhibitor activity / presynaptic active zone membrane / voltage-gated potassium channel complex / somatodendritic compartment / photoreceptor inner segment / ionotropic glutamate receptor binding / endomembrane system / acrosomal vesicle / axonogenesis / secretory granule / SNARE binding / synaptic transmission, glutamatergic / filopodium / PDZ domain binding / neuromuscular junction / locomotory behavior / intracellular protein transport / trans-Golgi network / postsynaptic density 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: 3.91 Å | ||||||||||||
![]() | White KI / Brunger AT | ||||||||||||
資金援助 | ![]()
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![]() | ジャーナル: bioRxiv / 年: 2025 タイトル: Structural remodeling of target-SNARE protein complexes by NSF enables synaptic transmission. 著者: K Ian White / Yousuf A Khan / Kangqiang Qiu / Ashwin Balaji / Sergio Couoh-Cardel / Luis Esquivies / Richard A Pfuetzner / Jiajie Diao / Axel T Brunger / ![]() 要旨: Synaptic vesicles containing neurotransmitters fuse with the plasma membrane upon the arrival of an action potential at the active zone. Multiple proteins organize trans-SNARE complex assembly and ...Synaptic vesicles containing neurotransmitters fuse with the plasma membrane upon the arrival of an action potential at the active zone. Multiple proteins organize trans-SNARE complex assembly and priming, leading to fusion. One target membrane SNARE, syntaxin, forms nanodomains at the active zone, and another, SNAP-25, enters non-fusogenic complexes with it. Here, we reveal mechanistic details of AAA+ protein NSF (N-ethylmaleimide sensitive factor) and SNAP (soluble NSF attachment protein) action before fusion. We show that syntaxin clusters are conserved, that NSF colocalizes with them, and characterize SNARE populations that may exist within or near them using cryo-EM. Supercomplexes of NSF, α-SNAP, and either a syntaxin tetramer or one of two binary complexes of syntaxin-SNAP-25 reveal atomic details of SNARE processing and show how sequential ATP hydrolysis drives disassembly. These results suggest a functional role for syntaxin clusters as reservoirs and a corresponding role for NSF in syntaxin liberation and SNARE protein quality control preceding fusion. | ||||||||||||
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構造の表示
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マップデータ | ![]() | 91.4 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 34.4 KB 34.4 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 9.7 KB | 表示 | ![]() |
画像 | ![]() | 146.4 KB | ||
Filedesc metadata | ![]() | 8.2 KB | ||
その他 | ![]() ![]() ![]() | 47.8 MB 89.9 MB 89.9 MB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 1 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 1 MB | 表示 | |
XML形式データ | ![]() | 18 KB | 表示 | |
CIF形式データ | ![]() | 23.1 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 | ![]() 9pbvMC ![]() 9ojrC ![]() 9ojuC ![]() 9ojzC ![]() 9ok3C ![]() 9ok5C ![]() 9okcC ![]() 9oljC ![]() 9oloC ![]() 9om6C ![]() 9omqC ![]() 9pafC ![]() 9pagC ![]() 9pb9C ![]() 9pbaC ![]() 9pbfC ![]() 9pc3C ![]() 9pcxC ![]() 9pczC ![]() 9pd1C ![]() 9pd8C ![]() 9pdbC ![]() 9pddC ![]() 9pf2C ![]() 9pfcC ![]() 9pffC ![]() 9pfgC M: このマップから作成された原子モデル 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
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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注釈 | Sharpened map from CryoSPARC NU-Refine, B = 121.7 | ||||||||||||||||||||||||||||||||||||
投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.096 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
-追加マップ: Unsharpened map from CryoSPARC NU-Refine
ファイル | emd_71491_additional_1.map | ||||||||||||
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注釈 | Unsharpened map from CryoSPARC NU-Refine | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: Half map A from CryoSPARC NU-Refine
ファイル | emd_71491_half_map_1.map | ||||||||||||
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注釈 | Half map A from CryoSPARC NU-Refine | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: Half map B from CryoSPARC NU-Refine
ファイル | emd_71491_half_map_2.map | ||||||||||||
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注釈 | Half map B from CryoSPARC NU-Refine | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
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試料の構成要素
+全体 : The 21bin20S complex of NSF, alphaSNAP, and the soluble 2:1 binar...
+超分子 #1: The 21bin20S complex of NSF, alphaSNAP, and the soluble 2:1 binar...
+超分子 #2: Subcomplex of alphaSNAP, syntaxin-1a, and SNAP-25
+超分子 #3: Homohexameric NSF
+超分子 #4: 2:1 binary complex of SNAP-25 and syntaxin-1a
+分子 #1: Vesicle-fusing ATPase
+分子 #2: Syntaxin-1A
+分子 #3: Synaptosomal-associated protein 25
+分子 #4: Alpha-soluble NSF attachment protein
+分子 #5: ADENOSINE-5'-TRIPHOSPHATE
+分子 #6: 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
濃度 | 15 mg/mL | ||||||||||||||||||
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緩衝液 | pH: 8 構成要素:
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グリッド | モデル: Quantifoil R1.2/1.3 / 材質: GOLD / メッシュ: 200 / 前処理 - タイプ: GLOW DISCHARGE | ||||||||||||||||||
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 298 K / 装置: FEI VITROBOT MARK IV |
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電子顕微鏡法
顕微鏡 | TFS KRIOS |
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撮影 | #0 - Image recording ID: 1 #0 - フィルム・検出器のモデル: GATAN K3 (6k x 4k) #0 - 平均電子線量: 31.56 e/Å2 / #1 - Image recording ID: 2 #1 - フィルム・検出器のモデル: GATAN K3 (6k x 4k) #1 - 平均電子線量: 36.76 e/Å2 / #2 - Image recording ID: 3 #2 - フィルム・検出器のモデル: GATAN K3 (6k x 4k) #2 - 平均電子線量: 35.48 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 / Cs: 2.7 mm / 最大 デフォーカス(公称値): 3.0 µm / 最小 デフォーカス(公称値): 1.0 µm / 倍率(公称値): 22500 |
試料ステージ | 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER ホルダー冷却材: NITROGEN |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |