+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 2fxo | ||||||
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タイトル | Structure of the human beta-myosin S2 fragment | ||||||
要素 | Myosin heavy chain, cardiac muscle beta isoformミオシン | ||||||
キーワード | CONTRACTILE PROTEIN / COILED COIL (DIMERIC / PARALLEL) / FAMILIAL HYPERTROPHIC CARDIOMYOPATHY / FHC-ASSOCIATED MUTANT E924K / THICK FILAMENT (ミオフィラメント) | ||||||
機能・相同性 | 機能・相同性情報 regulation of slow-twitch skeletal muscle fiber contraction / regulation of the force of skeletal muscle contraction / muscle myosin complex / muscle filament sliding / regulation of the force of heart contraction / transition between fast and slow fiber / myosin filament / myosin II complex / adult heart development / cardiac muscle hypertrophy in response to stress ...regulation of slow-twitch skeletal muscle fiber contraction / regulation of the force of skeletal muscle contraction / muscle myosin complex / muscle filament sliding / regulation of the force of heart contraction / transition between fast and slow fiber / myosin filament / myosin II complex / adult heart development / cardiac muscle hypertrophy in response to stress / myosin complex / sarcomere organization / microfilament motor activity / ventricular cardiac muscle tissue morphogenesis / myofibril / skeletal muscle contraction / striated muscle contraction / stress fiber / ATP metabolic process / cardiac muscle contraction / regulation of heart rate / sarcomere / muscle contraction / Z disc / actin filament binding / calmodulin binding / ATP binding / 細胞質 類似検索 - 分子機能 | ||||||
生物種 | Homo sapiens (ヒト) | ||||||
手法 | X線回折 / シンクロトロン / SAD WITH SEMI-BRUTE- FORCE MOLECULAR REPLACEMENT / 解像度: 2.5 Å | ||||||
データ登録者 | Blankenfeldt, W. / Thoma, N.H. / Wray, J.S. / Gautel, M. / Schlichting, I. | ||||||
引用 | ジャーナル: Proc Natl Acad Sci U S A / 年: 2006 タイトル: Crystal structures of human cardiac beta-myosin II S2-Delta provide insight into the functional role of the S2 subfragment. 著者: Wulf Blankenfeldt / Nicolas H Thomä / John S Wray / Mathias Gautel / Ilme Schlichting / 要旨: Myosin II is the major component of the muscle thick filament. It consists of two N-terminal S1 subfragments ("heads") connected to a long dimeric coiled-coil rod. The rod is in itself twofold ...Myosin II is the major component of the muscle thick filament. It consists of two N-terminal S1 subfragments ("heads") connected to a long dimeric coiled-coil rod. The rod is in itself twofold symmetric, but in the filament, the two heads point away from the filament surface and are therefore not equivalent. This breaking of symmetry requires the initial section of the rod, subfragment 2 (S2), to be relatively flexible. S2 is an important functional element, involved in various mechanisms by which the activity of smooth and striated muscle is regulated. We have determined crystal structures of the 126 N-terminal residues of S2 from human cardiac beta-myosin II (S2-Delta), of both WT and the disease-associated E924K mutant. S2-Delta is a straight parallel dimeric coiled coil, but the N terminus of one chain is disordered in WT-S2-Delta due to crystal contacts, indicative of unstable local structure. Bulky noncanonical side chains pack into a/d positions of S2-Delta's N terminus, leading to defined local asymmetry and axial stagger, which could induce nonequivalence of the S1 subfragments. Additionally, S2 possesses a conserved charge distribution with three prominent rings of negative potential within S2-Delta, the first of which may provide a binding interface for the "blocked head" of smooth muscle myosin in the OFF state. The observation that many disease-associated mutations affect the second negatively charged ring further suggests that charge interactions play an important role in regulation of cardiac muscle activity through myosin-binding protein C. #1: ジャーナル: J.Mol.Biol. / 年: 1999 タイトル: Mutations in Beta-Myosin S2 that Cause Familial Hypertrophic Cardiomyopathy (Fhc) Abolish the Interaction with the Regulatory Domain of Myosin-Binding Protein-C 著者: Gruen, M. / Gautel, M. #2: ジャーナル: Nature / 年: 2003 タイトル: Visualization of an Unstable Coiled Coil from the Scallop Myosin Rod 著者: Li, Y. / Brown, J.H. / Reshetnikova, L. / Blazsek, A. / Farkas, L. / Nyitray, L. / Cohen, C. | ||||||
履歴 |
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-構造の表示
構造ビューア | 分子: MolmilJmol/JSmol |
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-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 2fxo.cif.gz | 111 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb2fxo.ent.gz | 88.8 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 2fxo.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
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/fx/2fxo ftp://data.pdbj.org/pub/pdb/validation_reports/fx/2fxo | HTTPS FTP |
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-関連構造データ
-リンク
-集合体
登録構造単位 |
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2 |
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単位格子 |
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-要素
#1: タンパク質 | 分子量: 15106.145 Da / 分子数: 4 / 断片: DELTA-S2 FRAGMENT (838-963) / 変異: E924K / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 組織: HEART MUSCLE / 遺伝子: HSBMHC / プラスミド: PET / 生物種 (発現宿主): Escherichia coli / 発現宿主: Escherichia coli BL21 (大腸菌) / 株 (発現宿主): BL21 / 参照: UniProt: P12883 |
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-実験情報
-実験
実験 | 手法: X線回折 / 使用した結晶の数: 1 |
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-試料調製
結晶 | マシュー密度: 2.6 Å3/Da / 溶媒含有率: 52.3 % |
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結晶化 | 温度: 296 K / 手法: 蒸気拡散法, シッティングドロップ法 / pH: 7.5 詳細: PEG 3350, SODIUM ACETATE, TRIS-HCL, pH 7.50, VAPOR DIFFUSION, SITTING DROP, temperature 296K |
-データ収集
回折 | 平均測定温度: 100 K |
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放射光源 | 由来: シンクロトロン / サイト: ESRF / ビームライン: ID14-1 / 波長: 0.934 |
検出器 | タイプ: MARRESEARCH / 検出器: CCD / 日付: 2001年2月16日 |
放射 | モノクロメーター: DIAMOND / プロトコル: SINGLE WAVELENGTH / 単色(M)・ラウエ(L): M / 散乱光タイプ: x-ray |
放射波長 | 波長: 0.934 Å / 相対比: 1 |
反射 | 解像度: 2.5→20 Å / Num. obs: 20190 / % possible obs: 96 % / Observed criterion σ(I): -3 / 冗長度: 3.2 % / Biso Wilson estimate: 61 Å2 / Rsym value: 0.08 / Net I/σ(I): 9 |
反射 シェル | 解像度: 2.5→2.6 Å / 冗長度: 3.2 % / Mean I/σ(I) obs: 3.2 / Rsym value: 0.388 / % possible all: 96.6 |
-解析
ソフトウェア |
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精密化 | 構造決定の手法: SAD WITH SEMI-BRUTE- FORCE MOLECULAR REPLACEMENT 開始モデル: PDB ENTRY 1XNM 1xnm 解像度: 2.5→20 Å / Cor.coef. Fo:Fc: 0.922 / Cor.coef. Fo:Fc free: 0.876 / SU B: 20.647 / SU ML: 0.458 / TLS residual ADP flag: LIKELY RESIDUAL / 交差検証法: THROUGHOUT / ESU R: 0.891 / ESU R Free: 0.419 / 立体化学のターゲット値: MAXIMUM LIKELIHOOD 詳細: Hydrogens have been added in the riding positions. Target sigma values for restrained B-factor refinement have been relaxed to 10 A*A to reflect the special shape of the molecule. Atoms that ...詳細: Hydrogens have been added in the riding positions. Target sigma values for restrained B-factor refinement have been relaxed to 10 A*A to reflect the special shape of the molecule. Atoms that could not be located have been assigned a temperature factor of 500 A*A and occupancy value of 0 for better discernability.
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溶媒の処理 | イオンプローブ半径: 0.8 Å / 減衰半径: 0.8 Å / VDWプローブ半径: 1.4 Å / 溶媒モデル: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
原子変位パラメータ | Biso mean: 61.39 Å2
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精密化ステップ | サイクル: LAST / 解像度: 2.5→20 Å
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拘束条件 |
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LS精密化 シェル | 解像度: 2.5→2.56 Å / Total num. of bins used: 20 /
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精密化 TLS | T33: 0.1116 Å2 / 手法: refined / Refine-ID: X-RAY DIFFRACTION
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精密化 TLSグループ |
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