+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-28487 | |||||||||
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タイトル | Eag Kv channel with voltage sensor in the up conformation | |||||||||
マップデータ | ||||||||||
試料 |
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キーワード | voltage-gated potassium channel / MEMBRANE PROTEIN | |||||||||
機能・相同性 | 機能・相同性情報 Voltage gated Potassium channels / potassium channel complex / regulation of presynaptic cytosolic calcium ion concentration / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / delayed rectifier potassium channel activity / CaM pathway / parallel fiber to Purkinje cell synapse / Cam-PDE 1 activation / Sodium/Calcium exchangers / Reduction of cytosolic Ca++ levels ...Voltage gated Potassium channels / potassium channel complex / regulation of presynaptic cytosolic calcium ion concentration / voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential / delayed rectifier potassium channel activity / CaM pathway / parallel fiber to Purkinje cell synapse / Cam-PDE 1 activation / Sodium/Calcium exchangers / Reduction of cytosolic Ca++ levels / Calmodulin induced events / nuclear inner membrane / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / Activation of Ca-permeable Kainate Receptor / Loss of phosphorylation of MECP2 at T308 / CREB1 phosphorylation through the activation of Adenylate Cyclase / PKA activation / organelle localization by membrane tethering / negative regulation of high voltage-gated calcium channel activity / CaMK IV-mediated phosphorylation of CREB / autophagosome membrane docking / mitochondrion-endoplasmic reticulum membrane tethering / Glycogen breakdown (glycogenolysis) / regulation of synaptic vesicle exocytosis / positive regulation of cyclic-nucleotide phosphodiesterase activity / negative regulation of calcium ion export across plasma membrane / CLEC7A (Dectin-1) induces NFAT activation / phosphatidylinositol bisphosphate binding / Activation of RAC1 downstream of NMDARs / regulation of cardiac muscle cell action potential / positive regulation of ryanodine-sensitive calcium-release channel activity / regulation of cell communication by electrical coupling involved in cardiac conduction / Synthesis of IP3 and IP4 in the cytosol / negative regulation of peptidyl-threonine phosphorylation / Negative regulation of NMDA receptor-mediated neuronal transmission / Phase 0 - rapid depolarisation / Unblocking of NMDA receptors, glutamate binding and activation / startle response / negative regulation of ryanodine-sensitive calcium-release channel activity / adenylate cyclase activator activity / protein phosphatase activator activity / RHO GTPases activate PAKs / Ion transport by P-type ATPases / : / Uptake and function of anthrax toxins / Long-term potentiation / Regulation of MECP2 expression and activity / Calcineurin activates NFAT / catalytic complex / DARPP-32 events / regulation of cardiac muscle contraction / detection of calcium ion / Smooth Muscle Contraction / regulation of ryanodine-sensitive calcium-release channel activity / axolemma / cellular response to interferon-beta / RHO GTPases activate IQGAPs / calcium channel inhibitor activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / eNOS activation / Protein methylation / voltage-gated potassium channel complex / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / Activation of AMPK downstream of NMDARs / Ion homeostasis / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / : / titin binding / positive regulation of protein autophosphorylation / regulation of calcium-mediated signaling / sperm midpiece / 14-3-3 protein binding / potassium ion transmembrane transport / calcium channel complex / substantia nigra development / cellular response to calcium ion / Ras activation upon Ca2+ influx through NMDA receptor / sarcomere / regulation of heart rate / FCERI mediated Ca+2 mobilization / FCGR3A-mediated IL10 synthesis / protein serine/threonine kinase activator activity / regulation of membrane potential / VEGFR2 mediated vascular permeability / regulation of cytokinesis / VEGFR2 mediated cell proliferation / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / positive regulation of peptidyl-threonine phosphorylation / spindle microtubule / Translocation of SLC2A4 (GLUT4) to the plasma membrane / positive regulation of receptor signaling pathway via JAK-STAT / RAF activation / postsynaptic density membrane / Transcriptional activation of mitochondrial biogenesis / positive regulation of protein serine/threonine kinase activity / potassium ion transport / Stimuli-sensing channels / cellular response to type II interferon / spindle pole / response to calcium ion 類似検索 - 分子機能 | |||||||||
生物種 | Rattus norvegicus (ドブネズミ) / Homo sapiens (ヒト) | |||||||||
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 | |||||||||
データ登録者 | Mandala VS / MacKinnon R | |||||||||
資金援助 | 米国, 1件
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引用 | ジャーナル: Proc Natl Acad Sci U S A / 年: 2022 タイトル: Voltage-sensor movements in the Eag Kv channel under an applied electric field. 著者: Venkata Shiva Mandala / Roderick MacKinnon / 要旨: Voltage-dependent ion channels regulate the opening of their pores by sensing the membrane voltage. This process underlies the propagation of action potentials and other forms of electrical activity ...Voltage-dependent ion channels regulate the opening of their pores by sensing the membrane voltage. This process underlies the propagation of action potentials and other forms of electrical activity in cells. The voltage dependence of these channels is governed by the transmembrane displacement of the positive charged S4 helix within their voltage-sensor domains. We use cryo-electron microscopy to visualize this movement in the mammalian Eag voltage-dependent potassium channel in lipid membrane vesicles with a voltage difference across the membrane. Multiple structural configurations show that the applied electric field displaces S4 toward the cytoplasm by two helical turns, resulting in an extended interfacial helix near the inner membrane leaflet. The position of S4 in this down conformation is sterically incompatible with an open pore, thus explaining how movement of the voltage sensor at hyperpolarizing membrane voltages locks the pore shut in this kind of voltage-dependent K (K) channel. The structures solved in lipid bilayer vesicles detail the intricate interplay between K channels and membranes, from showing how arginines are stabilized deep within the membrane and near phospholipid headgroups, to demonstrating how the channel reshapes the inner leaflet of the membrane itself. | |||||||||
履歴 |
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-構造の表示
添付画像 |
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-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_28487.map.gz | 59.2 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-28487-v30.xml emd-28487.xml | 17.7 KB 17.7 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_28487_fsc.xml | 8.5 KB | 表示 | FSCデータファイル |
画像 | emd_28487.png | 103.5 KB | ||
Filedesc metadata | emd-28487.cif.gz | 5.9 KB | ||
その他 | emd_28487_additional_1.map.gz emd_28487_half_map_1.map.gz emd_28487_half_map_2.map.gz | 30.8 MB 59 MB 59 MB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-28487 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-28487 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_28487_validation.pdf.gz | 1.1 MB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_28487_full_validation.pdf.gz | 1.1 MB | 表示 | |
XML形式データ | emd_28487_validation.xml.gz | 16.2 KB | 表示 | |
CIF形式データ | emd_28487_validation.cif.gz | 21.1 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28487 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-28487 | HTTPS FTP |
-関連構造データ
-リンク
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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「今月の分子」の関連する項目 |
-マップ
ファイル | ダウンロード / ファイル: emd_28487.map.gz / 形式: CCP4 / 大きさ: 64 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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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: 1.08 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: #1
ファイル | emd_28487_additional_1.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #1
ファイル | emd_28487_half_map_1.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #2
ファイル | emd_28487_half_map_2.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-試料の構成要素
-全体 : Complex of Eag Kv channel bound to the inhibitor calmodulin-Ca2+
全体 | 名称: Complex of Eag Kv channel bound to the inhibitor calmodulin-Ca2+ |
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要素 |
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-超分子 #1: Complex of Eag Kv channel bound to the inhibitor calmodulin-Ca2+
超分子 | 名称: Complex of Eag Kv channel bound to the inhibitor calmodulin-Ca2+ 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: Rattus norvegicus (ドブネズミ) |
-分子 #1: Potassium voltage-gated channel subfamily H member 1
分子 | 名称: Potassium voltage-gated channel subfamily H member 1 タイプ: protein_or_peptide / ID: 1 / コピー数: 4 / 光学異性体: LEVO |
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由来(天然) | 生物種: Rattus norvegicus (ドブネズミ) |
分子量 | 理論値: 81.664094 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: LVAPQNTFLE NIVRRSNDTN FVLGNAQIVD WPIVYSNDGF CKLSGYHRAE VMQKSSACSF MYGELTDKDT VEKVRQTFEN YEMNSFEIL MYKKNRTPVW FFVKIAPIRN EQDKVVLFLC TFSDITAFKQ PIEDDSCKGW GKFARLTRAL TSSRGVLQQL A PSVQKGEN ...文字列: LVAPQNTFLE NIVRRSNDTN FVLGNAQIVD WPIVYSNDGF CKLSGYHRAE VMQKSSACSF MYGELTDKDT VEKVRQTFEN YEMNSFEIL MYKKNRTPVW FFVKIAPIRN EQDKVVLFLC TFSDITAFKQ PIEDDSCKGW GKFARLTRAL TSSRGVLQQL A PSVQKGEN VHKHSRLAEV LQLGSDILPQ YKQEAPKTPP HIILHYCVFK TTWDWIILIL TFYTAILVPY NVSFKTRQNN VA WLVVDSI VDVIFLVDIV LNFHTTFVGP AGEVISDPKL IRMNYLKTWF VIDLLSCLPY DVINAFENVD EGISSLFSSL KVV RLLRLG RVARKLDHYI EYGAAVLVLL VCVFGLAAHW MACIWYSIGD YEIFDEDTKT IRNNSWLYQL ALDIGTPYQF NGSG SGKWE GGPSKNSVYI SSLYFTMTSL TSVGFGNIAP STDIEKIFAV AIMMIGSLLY ATIFGNVTTI FQQMYANTNR YHEML NSVR DFLKLYQVPK GLSERVMDYI VSTWSMSRGI DTEKVLQICP KDMRADICVH LNRKVFKEHP AFRLASDGCL RALAME FQT VHCAPGDLIY HAGESVDSLC FVVSGSLEVI QDDEVVAILG KGDVFGDVFW KEATLAQSCA NVRALTYCDL HVIKRDA LQ KVLEFYTAFS HSFSRNLILT YNLRKRIVFR KISDVKREEE ERMKRKNEAP LILPPDHPVR RLFQRFRQQK E UniProtKB: Voltage-gated delayed rectifier potassium channel KCNH1 |
-分子 #2: Calmodulin-1
分子 | 名称: Calmodulin-1 / タイプ: protein_or_peptide / ID: 2 / コピー数: 4 / 光学異性体: LEVO |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
分子量 | 理論値: 16.063608 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: EEQIAEFKEA FSLFDKDGDG TITTKELGTV MRSLGQNPTE AELQDMINEV DADGNGTIDF PEFLTMMARK MKDTDSEEEI REAFRVFDK DGNGYISAAE LRHVMTNLGE KLTDEEVDEM IREADIDGDG QVNYEEFVQM MTA UniProtKB: Calmodulin-1 |
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
濃度 | 0.2 mg/mL |
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緩衝液 | pH: 8 |
グリッド | モデル: Quantifoil R1.2/1.3 / 材質: GOLD / メッシュ: 400 / 前処理 - タイプ: GLOW DISCHARGE / 前処理 - 時間: 22 sec. |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 293 K / 装置: FEI VITROBOT MARK IV |
-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 K3 BIOQUANTUM (6k x 4k) 平均電子線量: 60.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | 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): 2.0 µm / 最小 デフォーカス(公称値): 1.0 µm |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |