+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-7781 | |||||||||
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タイトル | Cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 2 | |||||||||
マップデータ | cardiac thin filament decorated with C0C1 fragment of mysoin binding protein C | |||||||||
試料 |
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キーワード | myosin binding protein C / MOTOR PROTEIN | |||||||||
機能・相同性 | 機能・相同性情報 basal body patch / C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / tight junction assembly / regulation of transepithelial transport / cardiac myofibril / morphogenesis of a polarized epithelium / regulation of striated muscle contraction / profilin binding ...basal body patch / C zone / regulation of muscle filament sliding / striated muscle myosin thick filament / tight junction assembly / regulation of transepithelial transport / cardiac myofibril / morphogenesis of a polarized epithelium / regulation of striated muscle contraction / profilin binding / protein localization to bicellular tight junction / structural constituent of postsynaptic actin cytoskeleton / Formation of annular gap junctions / dense body / Gap junction degradation / Cell-extracellular matrix interactions / regulation of stress fiber assembly / positive regulation of ATP-dependent activity / Striated Muscle Contraction / Adherens junctions interactions / ventricular cardiac muscle tissue morphogenesis / Interaction between L1 and Ankyrins / Sensory processing of sound by outer hair cells of the cochlea / Sensory processing of sound by inner hair cells of the cochlea / A band / structural constituent of muscle / regulation of synaptic vesicle endocytosis / apical junction complex / regulation of focal adhesion assembly / sarcomere organization / positive regulation of wound healing / myosin binding / myofibril / maintenance of blood-brain barrier / NuA4 histone acetyltransferase complex / myosin heavy chain binding / filamentous actin / Recycling pathway of L1 / ATPase activator activity / calyx of Held / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / RHOBTB2 GTPase cycle / phagocytic vesicle / heart morphogenesis / cardiac muscle contraction / titin binding / EPHB-mediated forward signaling / sarcomere / axonogenesis / platelet aggregation / cell motility / Translocation of SLC2A4 (GLUT4) to the plasma membrane / actin filament / RHO GTPases Activate Formins / FCGR3A-mediated phagocytosis / 加水分解酵素; 酸無水物に作用; 酸無水物に作用・細胞または細胞小器官の運動に関与 / Signaling by high-kinase activity BRAF mutants / MAP2K and MAPK activation / Schaffer collateral - CA1 synapse / cellular response to type II interferon / structural constituent of cytoskeleton / Regulation of actin dynamics for phagocytic cup formation / VEGFA-VEGFR2 Pathway / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / Signaling by BRAF and RAF1 fusions / cell-cell junction / Clathrin-mediated endocytosis / actin binding / angiogenesis / blood microparticle / cytoskeleton / cell adhesion / hydrolase activity / positive regulation of cell migration / axon / focal adhesion / ubiquitin protein ligase binding / synapse / positive regulation of gene expression / protein kinase binding / extracellular space / extracellular exosome / ATP binding / identical protein binding / membrane / nucleus / metal ion binding / plasma membrane / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
生物種 | 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: 11.0 Å | |||||||||
データ登録者 | Galkin VE / Schroeder GF | |||||||||
資金援助 | 米国, 1件
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引用 | ジャーナル: Structure / 年: 2018 タイトル: N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament. 著者: Cristina Risi / Betty Belknap / Eva Forgacs-Lonart / Samantha P Harris / Gunnar F Schröder / Howard D White / Vitold E Galkin / 要旨: Muscle contraction relies on interaction between myosin-based thick filaments and actin-based thin filaments. Myosin binding protein C (MyBP-C) is a key regulator of actomyosin interactions. Recent ...Muscle contraction relies on interaction between myosin-based thick filaments and actin-based thin filaments. Myosin binding protein C (MyBP-C) is a key regulator of actomyosin interactions. Recent studies established that the N'-terminal domains (NTDs) of MyBP-C can either activate or inhibit thin filaments, but the mechanism of their collective action is poorly understood. Cardiac MyBP-C (cMyBP-C) harbors an extra NTD, which is absent in skeletal isoforms of MyBP-C, and its role in regulation of cardiac contraction is unknown. Here we show that the first two domains of human cMyPB-C (i.e., C0 and C1) cooperate to activate the thin filament. We demonstrate that C1 interacts with tropomyosin via a positively charged loop and that this interaction, stabilized by the C0 domain, is required for thin filament activation by cMyBP-C. Our data reveal a mechanism by which cMyBP-C can modulate cardiac contraction and demonstrate a function of the C0 domain. | |||||||||
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_7781.map.gz | 2 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-7781-v30.xml emd-7781.xml | 17 KB 17 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_7781.png | 137.1 KB | ||
Filedesc metadata | emd-7781.cif.gz | 6 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-7781 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-7781 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_7781_validation.pdf.gz | 434.4 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_7781_full_validation.pdf.gz | 434 KB | 表示 | |
XML形式データ | emd_7781_validation.xml.gz | 5.3 KB | 表示 | |
CIF形式データ | emd_7781_validation.cif.gz | 5.9 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-7781 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-7781 | 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_7781.map.gz / 形式: CCP4 / 大きさ: 7.6 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | cardiac thin filament decorated with C0C1 fragment of mysoin binding protein C | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
投影像・断面図 | 画像のコントロール
画像は Spider により作成 これらの図は立方格子座標系で作成されたものです | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 2.1 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 : cardiac thin filament decorated with C0C1 fragment of cardiac myo...
全体 | 名称: cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 2 |
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要素 |
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-超分子 #1: cardiac thin filament decorated with C0C1 fragment of cardiac myo...
超分子 | 名称: cardiac thin filament decorated with C0C1 fragment of cardiac myosin binding protein C mode 2 タイプ: organelle_or_cellular_component / ID: 1 / 親要素: 0 / 含まれる分子: all |
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-超分子 #2: actin
超分子 | 名称: actin / タイプ: complex / ID: 2 / 親要素: 1 / 含まれる分子: #1 |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
-超分子 #3: myosin binding protein C
超分子 | 名称: myosin binding protein C / タイプ: complex / ID: 3 / 親要素: 1 / 含まれる分子: #2-#3 |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
-超分子 #4: tropomyosin
超分子 | 名称: tropomyosin / タイプ: complex / ID: 4 / 親要素: 1 / 含まれる分子: #4 |
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由来(天然) | 生物種: Homo sapiens (ヒト) |
-分子 #1: Actin, cytoplasmic 2
分子 | 名称: Actin, cytoplasmic 2 / タイプ: protein_or_peptide / ID: 1 / コピー数: 5 / 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: 41.838766 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG ...文字列: MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG YALPHAILRL DLAGRDLTDY LMKILTERGY SFTTTAEREI VRDIKEKLCY VALDFEQEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PEALFQPSFL GMESCGIHET TFNSIMKCDV DIRKDLYANT VLSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ISKQEYDESG PSIVHRKCF UniProtKB: Actin, cytoplasmic 2 |
-分子 #2: Myosin-binding protein C, cardiac-type
分子 | 名称: Myosin-binding protein C, cardiac-type / タイプ: protein_or_peptide / ID: 2 / コピー数: 6 / 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: 12.180806 KDa |
組換発現 | 生物種: Escherichia coli (大腸菌) |
配列 | 文字列: MDDPIGLFVM RPQDGEVTVG GSITFSARVA GASLLKPPVV KWFKGKWVDL SSKVGQHLQL HDSYDRASKV YLFELHITDA QPAFTGSYR CEVSTKDKFD CSNFNLTVHE UniProtKB: Myosin-binding protein C, cardiac-type |
-分子 #3: Myosin-binding protein C, cardiac-type
分子 | 名称: Myosin-binding protein C, cardiac-type / タイプ: protein_or_peptide / ID: 3 / コピー数: 5 / 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: 10.70606 KDa |
組換発現 | 生物種: Escherichia coli (大腸菌) |
配列 | 文字列: MPEPGKKPVS AFSKKPRSVE VAAGSPAVFE AETERAGVKV RWQRGGSDIS ASNKYGLATE GTRHTLTVRE VGPADQGSYA VIAGSSKVK FDLKVIEAEK AE UniProtKB: Myosin-binding protein C, cardiac-type |
-分子 #4: Tropomyosin
分子 | 名称: Tropomyosin / タイプ: protein_or_peptide / ID: 4 / 詳細: model / 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: 10.826337 KDa |
組換発現 | 生物種: Homo sapiens (ヒト) |
配列 | 文字列: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) ...文字列: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) |
-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 | helical array |
-試料調製
緩衝液 | pH: 7 |
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グリッド | 材質: COPPER / メッシュ: 300 / 支持フィルム - 材質: CARBON / 支持フィルム - トポロジー: LACEY / 前処理 - タイプ: PLASMA CLEANING / 前処理 - 時間: 15 sec. / 前処理 - 雰囲気: OTHER |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 95 % / チャンバー内温度: 294 K |
-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 II (4k x 4k) 検出モード: INTEGRATING / 平均電子線量: 20.0 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 |
-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: 27.5 Å 想定した対称性 - らせんパラメータ - ΔΦ: -166.6 ° 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: BACK PROJECTION / 解像度のタイプ: BY AUTHOR / 解像度: 11.0 Å / 解像度の算出法: FSC 0.143 CUT-OFF / ソフトウェア - 名称: SPIDER / ソフトウェア - 詳細: IHRSR / 使用した粒子像数: 5830 |
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初期モデル | モデルのタイプ: OTHER / 詳細: cylinder density map |
最終 角度割当 | タイプ: NOT APPLICABLE / ソフトウェア - 名称: SPIDER |
-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: Correlation coefficient |
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得られたモデル | PDB-6cxj: |