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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-4177 | |||||||||
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| タイトル | Cryo-EM structure of two dynein tail domains bound to dynactin and HOOK3 | |||||||||
マップデータ | Cryo-EM map showing two dynein tails bound to dynactin and HOOK3 | |||||||||
試料 |
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キーワード | TDH / DDH / Complex / dynein/dynactin/HOOK3 / MOTOR PROTEIN | |||||||||
| 機能・相同性 | 機能・相同性情報RHOD GTPase cycle / Factors involved in megakaryocyte development and platelet production / retrograde axonal transport of mitochondrion / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions / RHO GTPases Activate WASPs and WAVEs / MAP2K and MAPK activation ...RHOD GTPase cycle / Factors involved in megakaryocyte development and platelet production / retrograde axonal transport of mitochondrion / Regulation of actin dynamics for phagocytic cup formation / EPHB-mediated forward signaling / Adherens junctions interactions / VEGFA-VEGFR2 Pathway / Cell-extracellular matrix interactions / RHO GTPases Activate WASPs and WAVEs / MAP2K and MAPK activation / UCH proteinases / Gap junction degradation / Formation of annular gap junctions / RHOF GTPase cycle / Clathrin-mediated endocytosis / Formation of the dystrophin-glycoprotein complex (DGC) / dynactin complex / transport along microtubule / visual behavior / Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / F-actin capping protein complex / WASH complex / Recruitment of mitotic centrosome proteins and complexes / dynein light chain binding / dynein heavy chain binding / ciliary tip / cellular response to cytochalasin B / Intraflagellar transport / positive regulation of intracellular transport / regulation of transepithelial transport / regulation of metaphase plate congression / morphogenesis of a polarized epithelium / structural constituent of postsynaptic actin cytoskeleton / positive regulation of spindle assembly / barbed-end actin filament capping / protein localization to adherens junction / establishment of spindle localization / dense body / Neutrophil degranulation / postsynaptic actin cytoskeleton / Tat protein binding / coronary vasculature development / regulation of cell morphogenesis / dynein complex / adherens junction assembly / COPI-independent Golgi-to-ER retrograde traffic / retrograde axonal transport / apical protein localization / RHO GTPases activate IQGAPs / RHO GTPases Activate Formins / P-body assembly / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / microtubule motor activity / MHC class II antigen presentation / tight junction / Recruitment of NuMA to mitotic centrosomes / minus-end-directed microtubule motor activity / cytoplasmic dynein complex / dynein light intermediate chain binding / centrosome localization / COPI-mediated anterograde transport / aorta development / ventricular septum development / microtubule-based movement / nuclear migration / apical junction complex / regulation of norepinephrine uptake / transporter regulator activity / nitric-oxide synthase binding / cortical cytoskeleton / NuA4 histone acetyltransferase complex / establishment or maintenance of cell polarity / dynein intermediate chain binding / dynein complex binding / brush border / kinesin binding / regulation of synaptic vesicle endocytosis / microtubule-based process / regulation of protein localization to plasma membrane / positive regulation of double-strand break repair via homologous recombination / COPI-mediated anterograde transport / cytoplasmic microtubule / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / cytoplasmic microtubule organization / cytoskeleton organization / axon cytoplasm / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / stress granule assembly / Recruitment of mitotic centrosome proteins and complexes / MHC class II antigen presentation / Recruitment of NuMA to mitotic centrosomes / axonogenesis / Anchoring of the basal body to the plasma membrane 類似検索 - 分子機能 | |||||||||
| 生物種 | ![]() 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: 6.7 Å | |||||||||
データ登録者 | Lau CK / Urnavicius L | |||||||||
| 資金援助 | 英国, 2件
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引用 | ジャーナル: Nature / 年: 2018タイトル: Cryo-EM shows how dynactin recruits two dyneins for faster movement. 著者: Linas Urnavicius / Clinton K Lau / Mohamed M Elshenawy / Edgar Morales-Rios / Carina Motz / Ahmet Yildiz / Andrew P Carter / ![]() 要旨: Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. ...Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 Å resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine. | |||||||||
| 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: SurfView Molmil Jmol/JSmol |
| 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_4177.map.gz | 44.6 MB | EMDBマップデータ形式 | |
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| ヘッダ (付随情報) | emd-4177-v30.xml emd-4177.xml | 52 KB 52 KB | 表示 表示 | EMDBヘッダ |
| 画像 | emd_4177.png | 79.6 KB | ||
| Filedesc metadata | emd-4177.cif.gz | 10 KB | ||
| その他 | emd_4177_half_map_1.map.gz emd_4177_half_map_2.map.gz | 668.2 MB 669.7 MB | ||
| アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-4177 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4177 | HTTPS FTP |
-検証レポート
| 文書・要旨 | emd_4177_validation.pdf.gz | 327.2 KB | 表示 | EMDB検証レポート |
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| 文書・詳細版 | emd_4177_full_validation.pdf.gz | 326.4 KB | 表示 | |
| XML形式データ | emd_4177_validation.xml.gz | 17.8 KB | 表示 | |
| アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4177 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4177 | HTTPS FTP |
-関連構造データ
| 関連構造データ | ![]() 6f38MC ![]() 4168C ![]() 4169C ![]() 4170C ![]() 4171C ![]() 4172C ![]() 5owoC ![]() 6f1tC ![]() 6f1uC ![]() 6f1vC ![]() 6f1yC ![]() 6f1zC ![]() 6f3aC 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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| 類似構造データ |
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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 |
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マップ
| ファイル | ダウンロード / ファイル: emd_4177.map.gz / 形式: CCP4 / 大きさ: 824 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| 注釈 | Cryo-EM map showing two dynein tails bound to dynactin and HOOK3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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: 1.42 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
-ハーフマップ: #1
| ファイル | emd_4177_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_4177_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 |
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試料の構成要素
+全体 : Complex of two dynein tail domains bound to dynactin and HOOK3
+超分子 #1: Complex of two dynein tail domains bound to dynactin and HOOK3
+超分子 #2: Dynactin
+超分子 #3: Dynein
+超分子 #4: HOOK3
+分子 #1: ARP1 actin related protein 1 homolog A
+分子 #2: Actin, cytoplasmic 1
+分子 #3: Actin related protein 10 homolog
+分子 #4: Capping protein (Actin filament) muscle Z-line, alpha 1
+分子 #5: F-actin capping protein beta subunit
+分子 #6: Dynactin Subunit 2
+分子 #7: Dynactin Subunit 2
+分子 #8: Dynactin Subunit 3
+分子 #9: Dynactin Subunit 2
+分子 #10: Dynactin 6
+分子 #11: Dynactin subunit 5
+分子 #12: HOOK3
+分子 #13: Dynactin Subunit 4
+分子 #14: Dynactin Subunit 1
+分子 #15: Dynactin subunit 2
+分子 #16: Dynactin subunit 2
+分子 #17: Dynactin subunit 2
+分子 #18: Dynactin subunit 2
+分子 #19: Cytoplasmic dynein 1 heavy chain 1
+分子 #20: Cytoplasmic dynein 1 intermediate chain 2
+分子 #21: Cytoplasmic dynein 1 light intermediate chain 2
+分子 #22: Dynein light chain roadblock-type 1
+分子 #23: Dynactin Subunit 1
+分子 #24: ADENOSINE-5'-DIPHOSPHATE
+分子 #25: ADENOSINE-5'-TRIPHOSPHATE
-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 |
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試料調製
| 緩衝液 | pH: 7.2 |
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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: FEI FALCON III (4k x 4k) 検出モード: INTEGRATING / 平均電子線量: 45.0 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 |
| 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 EMDB ID: 詳細: Model low pass filtered to 50 Angstroms |
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| 最終 再構成 | 想定した対称性 - 点群: C1 (非対称) / 解像度のタイプ: BY AUTHOR / 解像度: 6.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 23407 |
| 初期 角度割当 | タイプ: PROJECTION MATCHING / ソフトウェア - 名称: RELION |
| 最終 角度割当 | タイプ: PROJECTION MATCHING / ソフトウェア - 名称: RELION |
-原子モデル構築 1
| 精密化 | 空間: REAL / プロトコル: FLEXIBLE FIT / 当てはまり具合の基準: Corellation Coefficient |
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| 得られたモデル | ![]() PDB-6f38: |
ムービー
コントローラー
万見について



キーワード
Homo sapiens (ヒト)
データ登録者
英国, 2件
引用

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