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基本情報
登録情報 | データベース: EMDB / ID: EMD-9697 | |||||||||
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タイトル | alpha-SNAP-SNARE subcomplex in the whole 20S complex | |||||||||
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![]() | membrane fusion / ATPase / MEMBRANE PROTEIN | |||||||||
機能・相同性 | ![]() soluble NSF attachment protein activity / trans-Golgi Network Vesicle Budding / BLOC-1 complex / SNARE complex disassembly / regulation of delayed rectifier potassium channel activity / myosin head/neck binding / exocytic insertion of neurotransmitter receptor to postsynaptic membrane / Other interleukin signaling / extrinsic component of presynaptic membrane / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex ...soluble NSF attachment protein activity / trans-Golgi Network Vesicle Budding / BLOC-1 complex / SNARE complex disassembly / regulation of delayed rectifier potassium channel activity / myosin head/neck binding / exocytic insertion of neurotransmitter receptor to postsynaptic membrane / Other interleukin signaling / extrinsic component of presynaptic membrane / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex / synaptobrevin 2-SNAP-25-syntaxin-1a complex / synaptic vesicle fusion to presynaptic active zone membrane / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex / Lysosome Vesicle Biogenesis / Glutamate Neurotransmitter Release Cycle / positive regulation of norepinephrine secretion / Norepinephrine Neurotransmitter Release Cycle / Acetylcholine Neurotransmitter Release Cycle / positive regulation of catecholamine secretion / zymogen granule membrane / Serotonin Neurotransmitter Release Cycle / GABA synthesis, release, reuptake and degradation / regulation of synaptic vesicle priming / Dopamine Neurotransmitter Release Cycle / Golgi Associated Vesicle Biogenesis / regulated exocytosis / presynaptic dense core vesicle exocytosis / ribbon synapse / synaptic vesicle docking / regulation of establishment of protein localization / storage vacuole / response to gravity / calcium ion-regulated exocytosis of neurotransmitter / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / positive regulation of calcium ion-dependent exocytosis / vesicle fusion / eosinophil degranulation / vesicle docking / chloride channel inhibitor activity / secretion by cell / SNARE complex / SNAP receptor activity / Cargo recognition for clathrin-mediated endocytosis / regulation of vesicle-mediated transport / Clathrin-mediated endocytosis / regulation of exocytosis / LGI-ADAM interactions / hormone secretion / calcium-ion regulated exocytosis / actomyosin / positive regulation of intracellular protein transport / Golgi to plasma membrane protein transport / positive regulation of hormone secretion / neurotransmitter secretion / neurotransmitter receptor internalization / ATP-dependent protein binding / protein localization to membrane / neuron projection terminus / regulation of synaptic vesicle recycling / neurotransmitter transport / insulin secretion / syntaxin binding / syntaxin-1 binding / SNARE complex assembly / positive regulation of neurotransmitter secretion / vacuolar membrane / clathrin-coated vesicle / Neutrophil degranulation / synaptic vesicle priming / endosomal transport / regulation of synapse assembly / postsynaptic cytosol / myosin binding / regulation of neuron projection development / exocytosis / voltage-gated potassium channel activity / positive regulation of exocytosis / synaptic vesicle exocytosis / modulation of excitatory postsynaptic potential / associative learning / positive regulation of excitatory postsynaptic potential / protein sumoylation / synaptic vesicle endocytosis / endomembrane system / calcium channel inhibitor activity / long-term memory / response to glucose / axonal growth cone / presynaptic active zone membrane / voltage-gated potassium channel complex / vesicle-mediated transport / somatodendritic compartment / photoreceptor inner segment / axonogenesis / acrosomal vesicle / SNARE binding / secretory granule / filopodium / synaptic transmission, glutamatergic / locomotory behavior 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: 3.9 Å | |||||||||
![]() | Huang X / Sun S | |||||||||
![]() | ![]() タイトル: Mechanistic insights into the SNARE complex disassembly. 著者: Xuan Huang / Shan Sun / Xiaojing Wang / Fenghui Fan / Qiang Zhou / Shan Lu / Yong Cao / Qiu-Wen Wang / Meng-Qiu Dong / Jun Yao / Sen-Fang Sui / ![]() 要旨: NSF (-ethylmaleimide-sensitive factor) and α-SNAP (α-soluble NSF attachment protein) bind to the SNARE (soluble NSF attachment protein receptor) complex, the minimum machinery to mediate membrane ...NSF (-ethylmaleimide-sensitive factor) and α-SNAP (α-soluble NSF attachment protein) bind to the SNARE (soluble NSF attachment protein receptor) complex, the minimum machinery to mediate membrane fusion, to form a 20S complex, which disassembles the SNARE complex for reuse. We report the cryo-EM structures of the α-SNAP-SNARE subcomplex and the NSF-D1D2 domain in the 20S complex at 3.9- and 3.7-Å resolutions, respectively. Combined with the biochemical and electrophysiological analyses, we find that α-SNAPs use R116 through electrostatic interactions and L197 through hydrophobic interactions to apply force mainly on two positions of the VAMP protein to execute disassembly process. Furthermore, we define the interaction between the amino terminus of the SNARE helical bundle and the pore loop of the NSF-D1 domain and demonstrate its essential role as a potential anchor for SNARE complex disassembly. Our studies provide a rotation model of α-SNAP-mediated disassembly of the SNARE complex. | |||||||||
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 | EMマップ: ![]() ![]() ![]() |
添付画像 |
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マップデータ | ![]() | 14.6 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 13.6 KB 13.6 KB | 表示 表示 | ![]() |
画像 | ![]() | 185.1 KB | ||
Filedesc metadata | ![]() | 5.8 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 | ![]() 6ip1MC ![]() 9698C ![]() 9723C ![]() 9724C ![]() 9725C ![]() 9726C ![]() 9727C ![]() 9728C ![]() 9729C ![]() 6ip2C 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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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: 1.30654 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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-添付データ
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試料の構成要素
-全体 : alpha-SNAP-SNARE subcomplex in the whole 20S complex
全体 | 名称: alpha-SNAP-SNARE subcomplex in the whole 20S complex |
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要素 |
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-超分子 #1: alpha-SNAP-SNARE subcomplex in the whole 20S complex
超分子 | 名称: alpha-SNAP-SNARE subcomplex in the whole 20S complex タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: all |
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由来(天然) | 生物種: ![]() ![]() |
-分子 #1: Vesicle-associated membrane protein 2
分子 | 名称: Vesicle-associated membrane protein 2 / タイプ: protein_or_peptide / ID: 1 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() ![]() |
分子量 | 理論値: 10.550823 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: GSHMSATAAT VPPAAPAGEG GPPAPPPNLT SNRRLQQTQA QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKR KYWWKNLK UniProtKB: Vesicle-associated membrane protein 2 |
-分子 #2: Syntaxin-1A
分子 | 名称: Syntaxin-1A / タイプ: protein_or_peptide / ID: 2 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() ![]() |
分子量 | 理論値: 29.363736 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: GSKDRTQELR TAKDSDDDDD VTVTVDRDRF MDEFFEQVEE IRGFIDKIAE NVEEVKRKHS AILASPNPDE KTKEELEELM SDIKKTANK VRSKLKSIEQ SIEQEEGLNR SSADLRIRKT QHSTLSRKFV EVMSEYNATQ SDYRERCKGR IQRQLEITGR T TTSEELED ...文字列: GSKDRTQELR TAKDSDDDDD VTVTVDRDRF MDEFFEQVEE IRGFIDKIAE NVEEVKRKHS AILASPNPDE KTKEELEELM SDIKKTANK VRSKLKSIEQ SIEQEEGLNR SSADLRIRKT QHSTLSRKFV EVMSEYNATQ SDYRERCKGR IQRQLEITGR T TTSEELED MLESGNPAIF ASGIIMDSSI SKQALSEIET RHSEIIKLEN SIRELHDMFM DMAMLVESQG EMIDRIEYNV EH AVDYVER AVSDTKK UniProtKB: Syntaxin-1A |
-分子 #3: Synaptosomal-associated protein 25
分子 | 名称: Synaptosomal-associated protein 25 / タイプ: protein_or_peptide / ID: 3 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() ![]() |
分子量 | 理論値: 11.571022 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: GSMAEDADMR NELEEMQRRA DQLADESLES TRRMLQLVEE SKDAGIRTLV MLDEQGEQLE RIEEGMDQIN KDMKEAEKNL TDLGKFCGL CVCPCNKLKS SDA UniProtKB: Synaptosomal-associated protein 25 |
-分子 #4: Synaptosomal-associated protein 25
分子 | 名称: Synaptosomal-associated protein 25 / タイプ: protein_or_peptide / ID: 4 / コピー数: 1 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() ![]() |
分子量 | 理論値: 9.277316 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: GSQMAISGGF IRRVTNDARE NEMDENLEQV SGIIGNLRHM ALDMGNEIDT QNRQIDRIME KADSNKTRID EANQRATKML GSG UniProtKB: Synaptosomal-associated protein 25 |
-分子 #5: Alpha-soluble NSF attachment protein
分子 | 名称: Alpha-soluble NSF attachment protein / タイプ: protein_or_peptide / ID: 5 / コピー数: 4 / 光学異性体: LEVO |
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由来(天然) | 生物種: ![]() ![]() |
分子量 | 理論値: 34.795332 KDa |
組換発現 | 生物種: ![]() ![]() |
配列 | 文字列: GSMRGSHHHH HHGSMDNSGK EAEAMALLAE AERKVKNSQS FFSGLFGGSS KIEEACEIYA RAANMFKMAK NWSAAGSAFC QAAQLHLQL QSKHDAATCF VDAGNAFKKA DPQEAINCLM RAIEIYTDMG RFTIAAKHHI SIAEIYETEL VDIEKAIAHY E QSADYYKG ...文字列: GSMRGSHHHH HHGSMDNSGK EAEAMALLAE AERKVKNSQS FFSGLFGGSS KIEEACEIYA RAANMFKMAK NWSAAGSAFC QAAQLHLQL QSKHDAATCF VDAGNAFKKA DPQEAINCLM RAIEIYTDMG RFTIAAKHHI SIAEIYETEL VDIEKAIAHY E QSADYYKG EESNSSANKC LLKVAGYAAQ LEQYQKAIDI YEQVGTNAMD SPLLKYSAKD YFFKAALCHF CIDMLNAKLA VQ KYEELFP AFSDSRECKL MKKLLEAHEE QNVDSYTEAV KEYDSISRLD QWLTTMLLRI KKTIQGDEED LR UniProtKB: NAPA protein |
-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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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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撮影 | フィルム・検出器のモデル: GATAN K2 SUMMIT (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 |
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: EMDB MAP |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 3.9 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 97910 |
初期 角度割当 | タイプ: RANDOM ASSIGNMENT |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD |