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データを開く
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基本情報
登録情報 | データベース: EMDB / ID: EMD-2685 | |||||||||
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タイトル | Density map of GluK2 desensitized state in complex with 2S,4R-4-methylglutamate | |||||||||
![]() | Reconstruction of GluK2 desensitized state | |||||||||
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![]() | Membrane Protein / Ion Channel / Glutamate Receptor | |||||||||
機能・相同性 | ![]() mossy fiber rosette / detection of cold stimulus involved in thermoception / Activation of Na-permeable kainate receptors / kainate selective glutamate receptor complex / Activation of Ca-permeable Kainate Receptor / negative regulation of synaptic transmission, glutamatergic / regulation of short-term neuronal synaptic plasticity / inhibitory postsynaptic potential / glutamate receptor activity / regulation of JNK cascade ...mossy fiber rosette / detection of cold stimulus involved in thermoception / Activation of Na-permeable kainate receptors / kainate selective glutamate receptor complex / Activation of Ca-permeable Kainate Receptor / negative regulation of synaptic transmission, glutamatergic / regulation of short-term neuronal synaptic plasticity / inhibitory postsynaptic potential / glutamate receptor activity / regulation of JNK cascade / ubiquitin conjugating enzyme binding / receptor clustering / modulation of excitatory postsynaptic potential / kainate selective glutamate receptor activity / ionotropic glutamate receptor complex / extracellularly glutamate-gated ion channel activity / neuronal action potential / behavioral fear response / positive regulation of synaptic transmission / glutamate-gated receptor activity / glutamate-gated calcium ion channel activity / ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / presynaptic modulation of chemical synaptic transmission / dendrite cytoplasm / hippocampal mossy fiber to CA3 synapse / regulation of membrane potential / SNARE binding / excitatory postsynaptic potential / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / synaptic transmission, glutamatergic / PDZ domain binding / postsynaptic density membrane / regulation of long-term neuronal synaptic plasticity / modulation of chemical synaptic transmission / terminal bouton / intracellular calcium ion homeostasis / positive regulation of neuron apoptotic process / presynaptic membrane / scaffold protein binding / chemical synaptic transmission / postsynaptic membrane / perikaryon / neuron apoptotic process / negative regulation of neuron apoptotic process / postsynaptic density / axon / neuronal cell body / ubiquitin protein ligase binding / glutamatergic synapse / synapse / dendrite / identical protein binding / membrane / 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: 7.6 Å | |||||||||
![]() | Meyerson JR / Kumar J / Chittori S / Rao P / Pierson J / Bartesaghi A / Mayer ML / Subramaniam S | |||||||||
![]() | ![]() タイトル: Structural mechanism of glutamate receptor activation and desensitization. 著者: Joel R Meyerson / Janesh Kumar / Sagar Chittori / Prashant Rao / Jason Pierson / Alberto Bartesaghi / Mark L Mayer / Sriram Subramaniam / ![]() 要旨: Ionotropic glutamate receptors are ligand-gated ion channels that mediate excitatory synaptic transmission in the vertebrate brain. To gain a better understanding of how structural changes gate ion ...Ionotropic glutamate receptors are ligand-gated ion channels that mediate excitatory synaptic transmission in the vertebrate brain. To gain a better understanding of how structural changes gate ion flux across the membrane, we trapped rat AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid) and kainate receptor subtypes in their major functional states and analysed the resulting structures using cryo-electron microscopy. We show that transition to the active state involves a 'corkscrew' motion of the receptor assembly, driven by closure of the ligand-binding domain. Desensitization is accompanied by disruption of the amino-terminal domain tetramer in AMPA, but not kainate, receptors with a two-fold to four-fold symmetry transition in the ligand-binding domains in both subtypes. The 7.6 Å structure of a desensitized kainate receptor shows how these changes accommodate channel closing. These findings integrate previous physiological, biochemical and structural analyses of glutamate receptors and provide a molecular explanation for key steps in receptor gating. | |||||||||
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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ダウンロードとリンク
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マップデータ | ![]() | 3.6 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 9.7 KB 9.7 KB | 表示 表示 | ![]() |
画像 | ![]() | 48.5 KB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 216.1 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 215.3 KB | 表示 | |
XML形式データ | ![]() | 5.8 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 | ![]() 4uqqMC ![]() 2680C ![]() 2684C ![]() 2686C ![]() 2687C ![]() 2688C ![]() 2689C ![]() 4uq6C ![]() 4uqjC ![]() 4uqkC 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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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 | Reconstruction of GluK2 desensitized state | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.406 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 : GluAK2 with 2S,4R-4-methylglutamate
全体 | 名称: GluAK2 with 2S,4R-4-methylglutamate |
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要素 |
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-超分子 #1000: GluAK2 with 2S,4R-4-methylglutamate
超分子 | 名称: GluAK2 with 2S,4R-4-methylglutamate / タイプ: sample / ID: 1000 / Number unique components: 2 |
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分子量 | 実験値: 400 KDa / 理論値: 400 KDa |
-分子 #1: GluK2
分子 | 名称: GluK2 / タイプ: protein_or_peptide / ID: 1 / 集合状態: Tetramer / 組換発現: Yes |
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由来(天然) | 生物種: ![]() ![]() |
分子量 | 実験値: 400 KDa / 理論値: 400 KDa |
組換発現 | 生物種: ![]() ![]() 組換細胞: Sf9 / 組換プラスミド: pFastBac1 |
配列 | UniProtKB: Glutamate receptor ionotropic, kainate 2 |
-分子 #2: 2S,4R-4-methylglutamate
分子 | 名称: 2S,4R-4-methylglutamate / タイプ: ligand / ID: 2 / 組換発現: No |
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由来(天然) | 生物種: synthetic construct (人工物) |
Chemical component information | ![]() ChemComp-SYM: |
-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 | 1.8 mg/mL |
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緩衝液 | pH: 8 詳細: 150 mM NaCl, 20 mM Tris pH 8.0, 0.75 mM DDM, 1 mM 2S,4R-4-methylglutamate |
グリッド | 詳細: Vitrified specimens were prepared by adding 2.5 uL of liganded protein at 1.8 mg/ml to R2/2 holey carbon grids (Quantifoil, Jena, Germany) rendered hydrophilic by chemical treatment to enable ...詳細: Vitrified specimens were prepared by adding 2.5 uL of liganded protein at 1.8 mg/ml to R2/2 holey carbon grids (Quantifoil, Jena, Germany) rendered hydrophilic by chemical treatment to enable particle distribution into the holes (Meyerson JR, Rao P, Kumar K, Chittori S, Banerjee S, Pierson J, Mayer ML, and Subramaniam S, manuscript in preparation). |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 120 K / 装置: FEI VITROBOT MARK IV / 手法: Blot for 2 seconds before plunging |
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電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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日付 | 2013年8月1日 |
撮影 | カテゴリ: CCD フィルム・検出器のモデル: FEI FALCON II (4k x 4k) 実像数: 4837 / 平均電子線量: 25 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 倍率(補正後): 47000 / 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): 3.5 µm / 最小 デフォーカス(公称値): 2.0 µm / 倍率(公称値): 47000 |
試料ステージ | 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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画像解析
詳細 | Particles were selected interactively at the computer terminal |
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CTF補正 | 詳細: Each particle |
最終 再構成 | 想定した対称性 - 点群: C2 (2回回転対称) / 解像度のタイプ: BY AUTHOR / 解像度: 7.6 Å / 解像度の算出法: OTHER / ソフトウェア - 名称: Relion / 使用した粒子像数: 21360 |