+
データを開く
-
基本情報
登録情報 | データベース: PDB / ID: 6mti | ||||||
---|---|---|---|---|---|---|---|
タイトル | Synaptotagmin-1 C2A, C2B domains and SNARE-pin proteins (5CCI) individually docked into Cryo-EM map of C2AB-SNARE complexes helically organized on lipid nanotube surface in presence of Mg2+ | ||||||
![]() |
| ||||||
![]() | EXOCYTOSIS / SNARE / lipid nanotubes | ||||||
機能・相同性 | ![]() exocytic insertion of neurotransmitter receptor to postsynaptic membrane / trans-Golgi Network Vesicle Budding / regulation of vesicle fusion / regulation of delayed rectifier potassium channel activity / synchronous neurotransmitter secretion / fast, calcium ion-dependent exocytosis of neurotransmitter / syntaxin-3 binding / spontaneous neurotransmitter secretion / regulation of regulated secretory pathway / positive regulation of vesicle fusion ...exocytic insertion of neurotransmitter receptor to postsynaptic membrane / trans-Golgi Network Vesicle Budding / regulation of vesicle fusion / regulation of delayed rectifier potassium channel activity / synchronous neurotransmitter secretion / fast, calcium ion-dependent exocytosis of neurotransmitter / syntaxin-3 binding / spontaneous neurotransmitter secretion / regulation of regulated secretory pathway / positive regulation of vesicle fusion / BLOC-1 complex / calcium-dependent activation of synaptic vesicle fusion / Lysosome Vesicle Biogenesis / myosin head/neck binding / positive regulation of calcium ion-dependent exocytosis of neurotransmitter / chromaffin granule membrane / zymogen granule membrane / storage vacuole / 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 / regulation of calcium ion-dependent exocytosis / Glutamate Neurotransmitter Release Cycle / calcium ion sensor activity / Norepinephrine Neurotransmitter Release Cycle / Acetylcholine Neurotransmitter Release Cycle / Serotonin Neurotransmitter Release Cycle / 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 / eosinophil degranulation / Golgi Associated Vesicle Biogenesis / regulation of synaptic vesicle priming / regulation of establishment of protein localization / vesicle-mediated transport in synapse / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / exocytic vesicle / positive regulation of intracellular protein transport / positive regulation of calcium ion-dependent exocytosis / vesicle organization / vesicle docking / protein heterooligomerization / ribbon synapse / positive regulation of dendrite extension / regulation of vesicle-mediated transport / Cargo recognition for clathrin-mediated endocytosis / secretion by cell / positive regulation of dopamine secretion / regulation of exocytosis / SNAP receptor activity / chloride channel inhibitor activity / SNARE complex / Clathrin-mediated endocytosis / vesicle fusion / calcium-ion regulated exocytosis / actomyosin / LGI-ADAM interactions / hormone secretion / dense core granule / Golgi to plasma membrane protein transport / positive regulation of hormone secretion / calcium-dependent phospholipid binding / neuron projection terminus / membraneless organelle assembly / ATP-dependent protein binding / neurotransmitter secretion / protein localization to membrane / regulation of synaptic vesicle recycling / syntaxin binding / clathrin-coated vesicle / presynaptic active zone / syntaxin-1 binding / insulin secretion / endosomal transport / Neutrophil degranulation / SNARE complex assembly / low-density lipoprotein particle receptor binding / positive regulation of neurotransmitter secretion / clathrin binding / neurotransmitter transport / phosphatidylserine binding / synaptic vesicle priming / regulation of synapse assembly / response to gravity / myosin binding / regulation of neuron projection development / regulation of dopamine secretion / regulation of synaptic vesicle exocytosis / exocytosis / modulation of excitatory postsynaptic potential / positive regulation of exocytosis / synaptic vesicle exocytosis 類似検索 - 分子機能 | ||||||
生物種 | ![]() ![]() | ||||||
手法 | 電子顕微鏡法 / らせん対称体再構成法 / クライオ電子顕微鏡法 / 解像度: 10.4 Å | ||||||
![]() | Grushin, K. / Wang, J. / Coleman, J. / Rothman, J. / Sindelar, C. / Krishnakumar, S. | ||||||
資金援助 | ![]()
| ||||||
![]() | ![]() タイトル: Structural basis for the clamping and Ca activation of SNARE-mediated fusion by synaptotagmin. 著者: Kirill Grushin / Jing Wang / Jeff Coleman / James E Rothman / Charles V Sindelar / Shyam S Krishnakumar / ![]() ![]() 要旨: Synapotagmin-1 (Syt1) interacts with both SNARE proteins and lipid membranes to synchronize neurotransmitter release to calcium (Ca) influx. Here we report the cryo-electron microscopy structure of ...Synapotagmin-1 (Syt1) interacts with both SNARE proteins and lipid membranes to synchronize neurotransmitter release to calcium (Ca) influx. Here we report the cryo-electron microscopy structure of the Syt1-SNARE complex on anionic-lipid containing membranes. Under resting conditions, the Syt1 C2 domains bind the membrane with a magnesium (Mg)-mediated partial insertion of the aliphatic loops, alongside weak interactions with the anionic lipid headgroups. The C2B domain concurrently interacts the SNARE bundle via the 'primary' interface and is positioned between the SNAREpins and the membrane. In this configuration, Syt1 is projected to sterically delay the complete assembly of the associated SNAREpins and thus, contribute to clamping fusion. This Syt1-SNARE organization is disrupted upon Ca-influx as Syt1 reorients into the membrane, likely displacing the attached SNAREpins and reversing the fusion clamp. We thus conclude that the cation (Mg/Ca) dependent membrane interaction is a key determinant of the dual clamp/activator function of Synaptotagmin-1. | ||||||
履歴 |
|
-
構造の表示
ムービー |
![]() |
---|---|
構造ビューア | 分子: ![]() ![]() |
-
ダウンロードとリンク
-
ダウンロード
PDBx/mmCIF形式 | ![]() | 574.3 KB | 表示 | ![]() |
---|---|---|---|---|
PDB形式 | ![]() | 473.8 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 | ![]() | 1.6 MB | 表示 | ![]() |
---|---|---|---|---|
文書・詳細版 | ![]() | 1.7 MB | 表示 | |
XML形式データ | ![]() | 96.2 KB | 表示 | |
CIF形式データ | ![]() | 136.6 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
-
リンク
-
集合体
登録構造単位 | ![]()
|
---|---|
1 |
|
-
要素
-Synaptotagmin- ... , 2種, 6分子 162345
#1: タンパク質 | 分子量: 14654.769 Da / 分子数: 2 / 断片: C2A domain, residues 141-267 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() #2: タンパク質 | 分子量: 32247.197 Da / 分子数: 4 / 断片: C2A and C2B domains, residues 141-421 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() |
---|
-タンパク質 , 2種, 12分子 AEIMQUBFJNRV
#3: タンパク質 | 分子量: 7231.061 Da / 分子数: 6 / 断片: residues 28-89 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() #4: タンパク質 | 分子量: 7837.957 Da / 分子数: 6 / 断片: residues 191-256 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() |
---|
-Synaptosomal-associated protein ... , 2種, 12分子 CGKOSWDHLPTX
#5: タンパク質 | 分子量: 9030.114 Da / 分子数: 6 / 断片: residues 7-83 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() #6: タンパク質 | 分子量: 7471.368 Da / 分子数: 6 / 断片: residues 141-204 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() |
---|
-非ポリマー , 1種, 10分子 
#7: 化合物 | ChemComp-MG / |
---|
-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
---|---|
EM実験 | 試料の集合状態: HELICAL ARRAY / 3次元再構成法: らせん対称体再構成法 |
-
試料調製
構成要素 | 名称: Synaptotagmin-1 C2A and C2B domains in the complex with SNARE proteins on the surface of lipid membrane nanotube タイプ: COMPLEX / Entity ID: #1-#6 / 由来: RECOMBINANT |
---|---|
由来(天然) | 生物種: ![]() ![]() |
由来(組換発現) | 生物種: ![]() ![]() |
緩衝液 | pH: 7.4 |
試料 | 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 |
-
電子顕微鏡撮影
実験機器 | ![]() モデル: Tecnai F20 / 画像提供: FEI Company |
---|---|
顕微鏡 | モデル: FEI TECNAI F20 |
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: 44 e/Å2 フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
-
解析
EMソフトウェア | 名称: Situs / カテゴリ: モデルフィッティング |
---|---|
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
らせん対称 | 回転角度/サブユニット: 78.48 ° / 軸方向距離/サブユニット: 7.3 Å / らせん対称軸の対称性: C1 |
3次元再構成 | 解像度: 10.4 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 2082 / 対称性のタイプ: HELICAL |
原子モデル構築 | プロトコル: RIGID BODY FIT |
原子モデル構築 | PDB-ID: 5CCI Accession code: 5CCI / Source name: PDB / タイプ: experimental model |