- EMDB-20721: Isolated cofilin bound to an actin filament -
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基本情報
登録情報
データベース: EMDB / ID: EMD-20721
タイトル
Isolated cofilin bound to an actin filament
マップデータ
Final unmasked map of isolated, bound cofilin segments selected from partially cofilin-decorated actin filaments. This map was low-pass filtered to 7.8 A and sharpened with a B-factor of -200.
試料
複合体: Complex of rabbit skeletal actin with isolated, bound human cofilin-1
複合体: Rabbit Skeletal Actin
タンパク質・ペプチド: Actin, alpha skeletal muscle
複合体: Human Cofilin-1
タンパク質・ペプチド: Cofilin-1
リガンド: MAGNESIUM ION
リガンド: ADENOSINE-5'-DIPHOSPHATE
キーワード
Cytoskeleton / STRUCTURAL PROTEIN
機能・相同性
機能・相同性情報
cellular response to ether / cofilin-actin rod / positive regulation of protein localization to cell leading edge / positive regulation of establishment of cell polarity regulating cell shape / negative regulation of unidimensional cell growth / positive regulation of barbed-end actin filament capping / neural fold formation / negative regulation of lamellipodium assembly / negative regulation of postsynaptic density organization / actin filament fragmentation ...cellular response to ether / cofilin-actin rod / positive regulation of protein localization to cell leading edge / positive regulation of establishment of cell polarity regulating cell shape / negative regulation of unidimensional cell growth / positive regulation of barbed-end actin filament capping / neural fold formation / negative regulation of lamellipodium assembly / negative regulation of postsynaptic density organization / actin filament fragmentation / positive regulation of actin filament depolymerization / positive regulation of embryonic development / modification of postsynaptic actin cytoskeleton / negative regulation of actin filament bundle assembly / positive regulation of synaptic plasticity / negative regulation of actin filament depolymerization / actin filament severing / establishment of spindle localization / negative regulation of cell motility / regulation of dendritic spine morphogenesis / host-mediated activation of viral process / cell projection organization / actin filament depolymerization / negative regulation of cell adhesion / RHO GTPases Activate ROCKs / negative regulation of cell size / cellular response to interleukin-6 / regulation of cell morphogenesis / negative regulation of dendritic spine maintenance / neural crest cell migration / positive regulation of cell motility / cytoskeletal motor activator activity / cellular response to insulin-like growth factor stimulus / cortical actin cytoskeleton / phosphatidylinositol bisphosphate binding / myosin heavy chain binding / tropomyosin binding / establishment of cell polarity / actin filament bundle / positive regulation of dendritic spine development / troponin I binding / filamentous actin / mesenchyme migration / mitotic cytokinesis / lamellipodium membrane / positive regulation of proteolysis / actin filament bundle assembly / skeletal muscle myofibril / striated muscle thin filament / skeletal muscle thin filament assembly / actin monomer binding / Sema3A PAK dependent Axon repulsion / cellular response to interleukin-1 / positive regulation of focal adhesion assembly / Rho protein signal transduction / response to amino acid / postsynaptic density, intracellular component / skeletal muscle fiber development / positive regulation of lamellipodium assembly / stress fiber / titin binding / actin filament polymerization / cytoskeleton organization / EPHB-mediated forward signaling / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / cellular response to epidermal growth factor stimulus / hippocampus development / response to activity / filopodium / actin filament / synaptic membrane / mitochondrial membrane / Regulation of actin dynamics for phagocytic cup formation / 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 / response to virus / ruffle membrane / nuclear matrix / cellular response to hydrogen peroxide / protein import into nucleus / calcium-dependent protein binding / actin filament binding / Platelet degranulation / cellular response to tumor necrosis factor / cell-cell junction / actin cytoskeleton / lamellipodium / actin cytoskeleton organization / cell body / positive regulation of cell growth / growth cone / protein phosphatase binding / vesicle / dendritic spine / hydrolase activity / protein domain specific binding / signaling receptor binding / focal adhesion / neuronal cell body / calcium ion binding / positive regulation of gene expression 類似検索 - 分子機能
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM097348
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM110533001
米国
引用
ジャーナル: Proc Natl Acad Sci U S A / 年: 2020 タイトル: Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments. 著者: Andrew R Huehn / Jeffrey P Bibeau / Anthony C Schramm / Wenxiang Cao / Enrique M De La Cruz / Charles V Sindelar / 要旨: Members of the cofilin/ADF family of proteins sever actin filaments, increasing the number of filament ends available for polymerization or depolymerization. Cofilin binds actin filaments with ...Members of the cofilin/ADF family of proteins sever actin filaments, increasing the number of filament ends available for polymerization or depolymerization. Cofilin binds actin filaments with positive cooperativity, forming clusters of contiguously bound cofilin along the filament lattice. Filament severing occurs preferentially at boundaries between bare and cofilin-decorated (cofilactin) segments and is biased at 1 side of a cluster. A molecular understanding of cooperative binding and filament severing has been impeded by a lack of structural data describing boundaries. Here, we apply methods for analyzing filament cryo-electron microscopy (cryo-EM) data at the single subunit level to directly investigate the structure of boundaries within partially decorated cofilactin filaments. Subnanometer resolution maps of isolated, bound cofilin molecules and an actin-cofilactin boundary indicate that cofilin-induced actin conformational changes are local and limited to subunits directly contacting bound cofilin. An isolated, bound cofilin compromises longitudinal filament contacts of 1 protofilament, consistent with a single cofilin having filament-severing activity. An individual, bound phosphomimetic (S3D) cofilin with weak severing activity adopts a unique binding mode that does not perturb actin structure. Cofilin clusters disrupt both protofilaments, consistent with a higher severing activity at boundaries compared to single cofilin. Comparison of these structures indicates that this disruption is substantially greater at pointed end sides of cofilactin clusters than at the barbed end. These structures, with the distribution of bound cofilin clusters, suggest that maximum binding cooperativity is achieved when 2 cofilins occupy adjacent sites. These results reveal the structural origins of cooperative cofilin binding and actin filament severing.
#241 - 2020年1月 20年の分子を振り返って (Twenty Years of Molecules) 類似性 (3)
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マップ
ファイル
ダウンロード / ファイル: emd_20721.map.gz / 形式: CCP4 / 大きさ: 40.6 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
注釈
Final unmasked map of isolated, bound cofilin segments selected from partially cofilin-decorated actin filaments. This map was low-pass filtered to 7.8 A and sharpened with a B-factor of -200.
フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 平均電子線量: 50.0 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: SPOT SCAN / 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
粒子像選択
選択した数: 1117338 詳細: Both bare and cofilin-decorated segments were selected and initially refined together.
初期モデル
モデルのタイプ: OTHER
最終 再構成
解像度のタイプ: BY AUTHOR / 解像度: 7.5 Å / 解像度の算出法: FSC 0.143 CUT-OFF 詳細: Filament segments with isolated, bound cofilin were split into even and odd halves for FSC calculations. 使用した粒子像数: 8917
初期 角度割当
タイプ: NOT APPLICABLE
最終 角度割当
タイプ: NOT APPLICABLE
最終 3次元分類
クラス数: 2 / 平均メンバー数/クラス: 559000 詳細: Particle subtraction and masking were used to restrict classification to a single subunit per boxed segment. Particles were sorted into a bare and cofilin-decorated class. Filaments were then ...詳細: Particle subtraction and masking were used to restrict classification to a single subunit per boxed segment. Particles were sorted into a bare and cofilin-decorated class. Filaments were then searched for isolated, bound cofilin.