+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-5170 | |||||||||
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タイトル | Binding of alpha-actinin CH1 to F-actin | |||||||||
マップデータ | reconstructed volume of F-actin decorated with alpha-actinin ABD (CH1 and CH2) | |||||||||
試料 |
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キーワード | helical filaments / calponin homology domains | |||||||||
機能・相同性 | 機能・相同性情報 positive regulation of glucose catabolic process to lactate via pyruvate / negative regulation of relaxation of muscle / regulation of the force of skeletal muscle contraction / skeletal muscle atrophy / positive regulation of skeletal muscle fiber development / positive regulation of norepinephrine uptake / positive regulation of skeletal muscle tissue growth / response to denervation involved in regulation of muscle adaptation / positive regulation of fast-twitch skeletal muscle fiber contraction / cellular response to cytochalasin B ...positive regulation of glucose catabolic process to lactate via pyruvate / negative regulation of relaxation of muscle / regulation of the force of skeletal muscle contraction / skeletal muscle atrophy / positive regulation of skeletal muscle fiber development / positive regulation of norepinephrine uptake / positive regulation of skeletal muscle tissue growth / response to denervation involved in regulation of muscle adaptation / positive regulation of fast-twitch skeletal muscle fiber contraction / cellular response to cytochalasin B / bBAF complex / npBAF complex / postsynaptic actin cytoskeleton organization / regulation of transepithelial transport / brahma complex / nBAF complex / structural constituent of postsynaptic actin cytoskeleton / morphogenesis of a polarized epithelium / GBAF complex / postsynaptic actin cytoskeleton / protein localization to adherens junction / Formation of annular gap junctions / regulation of G0 to G1 transition / dense body / positive regulation of bone mineralization involved in bone maturation / Gap junction degradation / Tat protein binding / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / regulation of double-strand break repair / transition between fast and slow fiber / muscle cell development / regulation of nucleotide-excision repair / RSC-type complex / apical protein localization / Prefoldin mediated transfer of substrate to CCT/TriC / adherens junction assembly / RHOF GTPase cycle / negative regulation of oxidative phosphorylation / focal adhesion assembly / Adherens junctions interactions / Striated Muscle Contraction / bone morphogenesis / 密着結合 / Sensory processing of sound by outer hair cells of the cochlea / SWI/SNF complex / Interaction between L1 and Ankyrins / negative regulation of glycolytic process / Sensory processing of sound by inner hair cells of the cochlea / regulation of mitotic metaphase/anaphase transition / Nephrin family interactions / regulation of norepinephrine uptake / negative regulation of cold-induced thermogenesis / positive regulation of double-strand break repair / positive regulation of T cell differentiation / NuA4 histone acetyltransferase complex / structural constituent of muscle / negative regulation of calcineurin-NFAT signaling cascade / regulation of synaptic vesicle endocytosis / apical junction complex / regulation of aerobic respiration / establishment or maintenance of cell polarity / maintenance of blood-brain barrier / cortical actin cytoskeleton / positive regulation of stem cell population maintenance / positive regulation of double-strand break repair via homologous recombination / cortical cytoskeleton / nitric-oxide synthase binding / regulation of cyclin-dependent protein serine/threonine kinase activity / Recycling pathway of L1 / 仮足 / regulation of G1/S transition of mitotic cell cycle / negative regulation of cell differentiation / 刷子縁 / kinesin binding / ヘルト萼状シナプス / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / positive regulation of myoblast differentiation / regulation of protein localization to plasma membrane / EPHB-mediated forward signaling / substantia nigra development / 軸索誘導 / negative regulation of protein binding / cell projection / 運動性 / マイクロフィラメント / Translocation of SLC2A4 (GLUT4) to the plasma membrane / RHO GTPases Activate Formins / regulation of transmembrane transporter activity / positive regulation of cell differentiation / FCGR3A-mediated phagocytosis / 接着結合 / 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 / DNA Damage Recognition in GG-NER / Signaling by high-kinase activity BRAF mutants / Schaffer collateral - CA1 synapse / MAP2K and MAPK activation / tau protein binding 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: 15.0 Å | |||||||||
データ登録者 | Galkin VE / Orlova A / Salmazo A / Djinovic-Carugo K / Egelman EH | |||||||||
引用 | ジャーナル: Nat Struct Mol Biol / 年: 2010 タイトル: Opening of tandem calponin homology domains regulates their affinity for F-actin. 著者: Vitold E Galkin / Albina Orlova / Anita Salmazo / Kristina Djinovic-Carugo / Edward H Egelman / 要旨: Many actin-binding proteins contain calponin homology (CH) domains, but the manner in which these domains interact with F-actin has been controversial. Crystal structures have shown the tandem CH ...Many actin-binding proteins contain calponin homology (CH) domains, but the manner in which these domains interact with F-actin has been controversial. Crystal structures have shown the tandem CH domains of alpha-actinin to be in a compact, closed conformation, but the interpretations of complexes of such tandem CH domains with F-actin have been ambiguous. We show that the tandem CH domains of alpha-actinin bind F-actin in an open conformation, explaining mutations that cause human diseases and suggesting that the opening of these domains may be one of the main regulatory mechanisms for proteins with tandem CH domains. | |||||||||
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_5170.map.gz | 3.5 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-5170-v30.xml emd-5170.xml | 8.7 KB 8.7 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_5170_1.jpg | 62.3 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-5170 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-5170 | 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_5170.map.gz / 形式: CCP4 / 大きさ: 3.7 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | reconstructed volume of F-actin decorated with alpha-actinin ABD (CH1 and CH2) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 2.38 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 : F-actin decorated with alpha-actinin ABD (containing CH1 and CH2)
全体 | 名称: F-actin decorated with alpha-actinin ABD (containing CH1 and CH2) |
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要素 |
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-超分子 #1000: F-actin decorated with alpha-actinin ABD (containing CH1 and CH2)
超分子 | 名称: F-actin decorated with alpha-actinin ABD (containing CH1 and CH2) タイプ: sample / ID: 1000 / 詳細: none / 集合状態: one to one binding / Number unique components: 2 |
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-分子 #1: F-actin
分子 | 名称: F-actin / タイプ: protein_or_peptide / ID: 1 / Name.synonym: F-actin / 集合状態: helical polymer / 組換発現: Yes |
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由来(天然) | 生物種: Homo sapiens (ヒト) / 別称: Human / 組織: muscle |
組換発現 | 生物種: Escherichia coli (大腸菌) |
配列 | GO: actin filament binding |
-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
凍結 | 凍結剤: ETHANE / 装置: OTHER |
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-電子顕微鏡法
顕微鏡 | FEI TECNAI F20 |
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電子線 | 加速電圧: 200 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 FIELDBright-field microscopy / 倍率(公称値): 50000 |
試料ステージ | 試料ホルダー: Gatan 626 / 試料ホルダーモデル: GATAN LIQUID NITROGEN |
撮影 | カテゴリ: FILM / フィルム・検出器のモデル: KODAK SO-163 FILM / デジタル化 - スキャナー: NIKON COOLSCAN / デジタル化 - サンプリング間隔: 12.7 µm / ビット/ピクセル: 16 |
実験機器 | モデル: Tecnai F20 / 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: 27.7 Å 想定した対称性 - らせんパラメータ - ΔΦ: 166.8 ° アルゴリズム: OTHER / 解像度のタイプ: BY AUTHOR / 解像度: 15.0 Å / 解像度の算出法: FSC 0.5 CUT-OFF / ソフトウェア - 名称: IHRSR |
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