+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-7771 | |||||||||
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タイトル | Cryo-EM reconstruction of microtubule-bound synthetic (R2x4) tau | |||||||||
マップデータ | Cryo-EM reconstruction of microtubule-bound synthetic tau (R2x4) | |||||||||
試料 |
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キーワード | microtubule / tau / STRUCTURAL PROTEIN | |||||||||
機能・相同性 | 機能・相同性情報 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Hedgehog 'off' state / Cilium Assembly / Intraflagellar transport / COPI-dependent Golgi-to-ER retrograde traffic / Carboxyterminal post-translational modifications of tubulin / RHOH GTPase cycle / Sealing of the nuclear envelope (NE) by ESCRT-III / Kinesins / PKR-mediated signaling ...Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane / Hedgehog 'off' state / Cilium Assembly / Intraflagellar transport / COPI-dependent Golgi-to-ER retrograde traffic / Carboxyterminal post-translational modifications of tubulin / RHOH GTPase cycle / Sealing of the nuclear envelope (NE) by ESCRT-III / Kinesins / PKR-mediated signaling / The role of GTSE1 in G2/M progression after G2 checkpoint / Aggrephagy / Resolution of Sister Chromatid Cohesion / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Separation of Sister Chromatids / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / Recruitment of NuMA to mitotic centrosomes / COPI-mediated anterograde transport / plus-end-directed organelle transport along microtubule / histone-dependent DNA binding / neurofibrillary tangle assembly / positive regulation of diacylglycerol kinase activity / axonal transport / negative regulation of establishment of protein localization to mitochondrion / neurofibrillary tangle / positive regulation of protein localization to synapse / microtubule lateral binding / tubulin complex / phosphatidylinositol bisphosphate binding / main axon / negative regulation of kinase activity / regulation of long-term synaptic depression / negative regulation of tubulin deacetylation / generation of neurons / rRNA metabolic process / internal protein amino acid acetylation / regulation of chromosome organization / regulation of mitochondrial fission / axonal transport of mitochondrion / intracellular distribution of mitochondria / axon development / central nervous system neuron development / regulation of microtubule polymerization / apolipoprotein binding / microtubule polymerization / lipoprotein particle binding / minor groove of adenine-thymine-rich DNA binding / dynactin binding / negative regulation of mitochondrial membrane potential / glial cell projection / protein polymerization / axolemma / negative regulation of mitochondrial fission / regulation of microtubule polymerization or depolymerization / Caspase-mediated cleavage of cytoskeletal proteins / positive regulation of axon extension / regulation of microtubule cytoskeleton organization / Activation of AMPK downstream of NMDARs / regulation of cellular response to heat / positive regulation of protein localization / cytoplasmic microtubule organization / stress granule assembly / supramolecular fiber organization / regulation of calcium-mediated signaling / axon cytoplasm / somatodendritic compartment / positive regulation of microtubule polymerization / synapse assembly / cellular response to brain-derived neurotrophic factor stimulus / nuclear periphery / phosphatidylinositol binding / cellular response to nerve growth factor stimulus / positive regulation of superoxide anion generation / protein phosphatase 2A binding / regulation of autophagy / astrocyte activation / response to lead ion / microglial cell activation / synapse organization / Hsp90 protein binding / protein homooligomerization / PKR-mediated signaling / regulation of synaptic plasticity / : / structural constituent of cytoskeleton / memory / SH3 domain binding / microtubule cytoskeleton organization / cytoplasmic ribonucleoprotein granule / cellular response to reactive oxygen species / microtubule cytoskeleton / neuron projection development / cell-cell signaling / protein-folding chaperone binding / mitotic cell cycle / single-stranded DNA binding 類似検索 - 分子機能 | |||||||||
生物種 | Sus scrofa (ブタ) / Homo sapiens (ヒト) | |||||||||
手法 | らせん対称体再構成法 / クライオ電子顕微鏡法 / 解像度: 3.9 Å | |||||||||
データ登録者 | Nogales E / Kellogg EH | |||||||||
資金援助 | 米国, 1件
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引用 | ジャーナル: Science / 年: 2018 タイトル: Near-atomic model of microtubule-tau interactions. 著者: Elizabeth H Kellogg / Nisreen M A Hejab / Simon Poepsel / Kenneth H Downing / Frank DiMaio / Eva Nogales / 要旨: Tau is a developmentally regulated axonal protein that stabilizes and bundles microtubules (MTs). Its hyperphosphorylation is thought to cause detachment from MTs and subsequent aggregation into ...Tau is a developmentally regulated axonal protein that stabilizes and bundles microtubules (MTs). Its hyperphosphorylation is thought to cause detachment from MTs and subsequent aggregation into fibrils implicated in Alzheimer's disease. It is unclear which tau residues are crucial for tau-MT interactions, where tau binds on MTs, and how it stabilizes them. We used cryo-electron microscopy to visualize different tau constructs on MTs and computational approaches to generate atomic models of tau-tubulin interactions. The conserved tubulin-binding repeats within tau adopt similar extended structures along the crest of the protofilament, stabilizing the interface between tubulin dimers. Our structures explain the effect of phosphorylation on MT affinity and lead to a model of tau repeats binding in tandem along protofilaments, tethering together tubulin dimers and stabilizing polymerization interfaces. | |||||||||
履歴 |
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-構造の表示
ムービー |
ムービービューア |
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構造ビューア | EMマップ: SurfViewMolmilJmol/JSmol |
添付画像 |
-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_7771.map.gz | 278.3 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-7771-v30.xml emd-7771.xml | 19.7 KB 19.7 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_7771.png | 152.3 KB | ||
Filedesc metadata | emd-7771.cif.gz | 7.1 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-7771 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-7771 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_7771_validation.pdf.gz | 645.7 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_7771_full_validation.pdf.gz | 645.2 KB | 表示 | |
XML形式データ | emd_7771_validation.xml.gz | 7.4 KB | 表示 | |
CIF形式データ | emd_7771_validation.cif.gz | 8.5 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-7771 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-7771 | 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_7771.map.gz / 形式: CCP4 / 大きさ: 307.5 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Cryo-EM reconstruction of microtubule-bound synthetic tau (R2x4) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 1.32 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
-試料の構成要素
+全体 : Ternary complex of alpha-beta tubulin with synthetic (R2x4) tau
+超分子 #1: Ternary complex of alpha-beta tubulin with synthetic (R2x4) tau
+超分子 #2: Tubulin beta chain
+超分子 #3: Tubulin alpha-1B chain
+超分子 #4: Microtubule-associated protein tau
+分子 #1: Tubulin beta chain
+分子 #2: Tubulin alpha-1B chain
+分子 #3: Microtubule-associated protein tau
+分子 #4: GUANOSINE-5'-DIPHOSPHATE
+分子 #5: GUANOSINE-5'-TRIPHOSPHATE
+分子 #6: MAGNESIUM ION
-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 | らせん対称体再構成法 |
試料の集合状態 | filament |
-試料調製
濃度 | 0.5 mg/mL | ||||||||||||||||||
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緩衝液 | pH: 6.8 構成要素:
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グリッド | モデル: C-flat-1.2/1.3 4C / 材質: COPPER / メッシュ: 400 / 支持フィルム - 材質: CARBON / 支持フィルム - トポロジー: HOLEY / 前処理 - タイプ: GLOW DISCHARGE / 前処理 - 時間: 10 sec. / 前処理 - 雰囲気: AIR | ||||||||||||||||||
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 310.15 K / 装置: FEI VITROBOT MARK IV 詳細: blot force 10 pN, 6 second blot time. used C-flat 1.2/1.3 holey grids. First 2 uL of microtubules were adhered to grid for 30 seconds, followed by 2 4 uL washes of tau with 30 second incubation for each wash.. | ||||||||||||||||||
詳細 | tubulin concentration is 0.5 mg/mL, tau concentration is 1 mg/mL |
-電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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特殊光学系 | 位相板: VOLTA PHASE PLATE |
撮影 | フィルム・検出器のモデル: GATAN K2 BASE (4k x 4k) 撮影したグリッド数: 1 / 実像数: 812 / 平均露光時間: 10.0 sec. / 平均電子線量: 40.5 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | C2レンズ絞り径: 100.0 µm / 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm / 最小 デフォーカス(公称値): 0.5 µm / 倍率(公称値): 37878 |
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 |
-画像解析
最終 再構成 | 想定した対称性 - らせんパラメータ - Δz: 8.7 Å 想定した対称性 - らせんパラメータ - ΔΦ: -25.75 ° 想定した対称性 - らせんパラメータ - 軸対称性: C1 (非対称) アルゴリズム: FOURIER SPACE / 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 / ソフトウェア - 名称: FREALIGN (ver. 9.09) / 使用した粒子像数: 19505 |
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Segment selection | 選択した数: 24571 / ソフトウェア - 名称: Appion |
初期モデル | モデルのタイプ: EMDB MAP EMDB ID: 詳細: used naked microtubule reconstruction as initial model, low-pass filtered to 20 Angstrom |
最終 角度割当 | タイプ: NOT APPLICABLE / ソフトウェア - 名称: FREALIGN (ver. 9.09) |
-原子モデル構築 1
精密化 | 空間: REAL / プロトコル: FLEXIBLE FIT / 温度因子: 120 / 当てはまり具合の基準: real space correlation |
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得られたモデル | PDB-6cvn: |