+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 3lue | ||||||
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タイトル | Model of alpha-actinin CH1 bound to F-actin | ||||||
要素 |
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キーワード | STRUCTURAL PROTEIN / calponin homology domains / Acetylation / ATP-binding / Cytoplasm / Cytoskeleton / Methylation / Nucleotide-binding / Phosphoprotein / Actin-binding / Calcium / Polymorphism / Deafness / Disease mutation / Dystonia | ||||||
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 skeletal muscle tissue growth / response to denervation involved in regulation of muscle adaptation / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / positive regulation of fast-twitch skeletal muscle fiber contraction ...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 skeletal muscle tissue growth / response to denervation involved in regulation of muscle adaptation / positive regulation of norepinephrine uptake / cellular response to cytochalasin B / positive regulation of fast-twitch skeletal muscle fiber contraction / regulation of transepithelial transport / morphogenesis of a polarized epithelium / bBAF complex / postsynaptic actin cytoskeleton organization / npBAF complex / nBAF complex / protein localization to adherens junction / brahma complex / postsynaptic actin cytoskeleton / Tat protein binding / structural constituent of postsynaptic actin cytoskeleton / transition between fast and slow fiber / positive regulation of bone mineralization involved in bone maturation / GBAF complex / dense body / Formation of annular gap junctions / regulation of G0 to G1 transition / Gap junction degradation / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / apical protein localization / muscle cell development / regulation of double-strand break repair / adherens junction assembly / regulation of nucleotide-excision repair / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / negative regulation of oxidative phosphorylation / focal adhesion assembly / RHOF GTPase cycle / Regulation of MITF-M-dependent genes involved in pigmentation / Adherens junctions interactions / Striated Muscle Contraction / tight junction / bone morphogenesis / negative regulation of glycolytic process / Nephrin family interactions / Sensory processing of sound by outer hair cells of the cochlea / regulation of norepinephrine uptake / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / regulation of mitotic metaphase/anaphase transition / negative regulation of cold-induced thermogenesis / SWI/SNF complex / positive regulation of double-strand break repair / regulation of synaptic vesicle endocytosis / positive regulation of T cell differentiation / apical junction complex / structural constituent of muscle / negative regulation of calcineurin-NFAT signaling cascade / regulation of aerobic respiration / establishment or maintenance of cell polarity / cortical actin cytoskeleton / regulation of cyclin-dependent protein serine/threonine kinase activity / maintenance of blood-brain barrier / cortical cytoskeleton / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / nitric-oxide synthase binding / pseudopodium / regulation of G1/S transition of mitotic cell cycle / Recycling pathway of L1 / kinesin binding / brush border / calyx of Held / negative regulation of cell differentiation / positive regulation of double-strand break repair via homologous recombination / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / regulation of protein localization to plasma membrane / positive regulation of myoblast differentiation / EPHB-mediated forward signaling / substantia nigra development / axonogenesis / negative regulation of protein binding / cell projection / Translocation of SLC2A4 (GLUT4) to the plasma membrane / actin filament / cell motility / RHO GTPases Activate Formins / positive regulation of cell differentiation / adherens junction / FCGR3A-mediated phagocytosis / regulation of transmembrane transporter activity / 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 / DNA Damage Recognition in GG-NER / MAP2K and MAPK activation / B-WICH complex positively regulates rRNA expression 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
手法 | 電子顕微鏡法 / らせん対称体再構成法 / クライオ電子顕微鏡法 / 解像度: 15 Å | ||||||
データ登録者 | Galkin, V.E. / Orlova, A. / Salmazo, A. / Djinovic-Carugo, K. / Egelman, E.H. | ||||||
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 | 分子: MolmilJmol/JSmol |
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 3lue.cif.gz | 824.1 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb3lue.ent.gz | 640.8 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 3lue.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 3lue_validation.pdf.gz | 861.1 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 3lue_full_validation.pdf.gz | 1.3 MB | 表示 | |
XML形式データ | 3lue_validation.xml.gz | 184.5 KB | 表示 | |
CIF形式データ | 3lue_validation.cif.gz | 254.2 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/lu/3lue ftp://data.pdbj.org/pub/pdb/validation_reports/lu/3lue | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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詳細 | Authors state that the model is from a continuous helix where the rotation per subunit is -167.2 degrees and the rise per subunit is 26.6 Angstroms. |
-要素
#1: タンパク質 | 分子量: 41651.465 Da / 分子数: 10 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: ACTB / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: P60709 #2: タンパク質 | 分子量: 12471.712 Da / 分子数: 10 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: ACTN3 / 発現宿主: Escherichia coli (大腸菌) / 参照: UniProt: Q08043 |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: FILAMENT / 3次元再構成法: らせん対称体再構成法 |
-試料調製
構成要素 |
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試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||
急速凍結 | 凍結剤: ETHANE |
-電子顕微鏡撮影
実験機器 | モデル: Tecnai F20 / 画像提供: FEI Company |
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顕微鏡 | モデル: FEI TECNAI F20 |
電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 200 kV / 照射モード: FLOOD BEAM |
電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 50000 X / カメラ長: 0 mm |
試料ホルダ | 試料ホルダーモデル: GATAN LIQUID NITROGEN / 資料ホルダタイプ: gatan 626 / 傾斜角・最大: 0 ° / 傾斜角・最小: 0 ° |
撮影 | フィルム・検出器のモデル: KODAK SO-163 FILM |
画像スキャン | サンプリングサイズ: 12.7 µm / Scanner model: NIKON COOLSCAN |
-解析
EMソフトウェア |
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CTF補正 | 詳細: Weiner filter | ||||||||||||
らせん対称 | 回転角度/サブユニット: 166.8 ° / 軸方向距離/サブユニット: 27.7 Å / らせん対称軸の対称性: C1 | ||||||||||||
3次元再構成 | 手法: back projection / 解像度: 15 Å / 解像度の算出法: FSC 0.5 CUT-OFF / ピクセルサイズ(公称値): 2.38 Å / ピクセルサイズ(実測値): 2.38 Å 詳細: AUTHORS STATE THAT THE STRANGE C-N BONDS WERE THE RESULT OF BREAKING THE CHAINS AT THESE POINTS TO DO RIGID BODY FITTING OF THE SUBDOMAINS. 対称性のタイプ: HELICAL | ||||||||||||
原子モデル構築 | プロトコル: OTHER / 空間: REAL 詳細: METHOD--both manually and with Chimera DETAILS--AUTHORS STATE THAT THE STRANGE C-N BONDS WERE THE RESULT OF BREAKING THE CHAINS AT THESE POINTS TO DO RIGID BODY FITTING OF THE SUBDOMAINS. | ||||||||||||
精密化ステップ | サイクル: LAST
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