登録情報 データベース : EMDB / ID : EMD-16304 ダウンロードとリンクタイトル In situ outer dynein arm from Chlamydomonas reinhardtii in a pre-power stroke state マップデータ 詳細 試料細胞器官・細胞要素 : In situ outer dynein armタンパク質・ペプチド : x 2種リガンド : x 2種 詳細 キーワード axoneme / outer dynein arm / pre power stroke / dynein / MOTOR PROTEIN機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
outer dynein arm / axonemal dynein complex / outer dynein arm assembly / dynein light chain binding / cilium movement / dynein heavy chain binding / dynein complex / minus-end-directed microtubule motor activity / dynein light intermediate chain binding / cytoplasmic dynein complex ... outer dynein arm / axonemal dynein complex / outer dynein arm assembly / dynein light chain binding / cilium movement / dynein heavy chain binding / dynein complex / minus-end-directed microtubule motor activity / dynein light intermediate chain binding / cytoplasmic dynein complex / motile cilium / dynein intermediate chain binding / microtubule-based movement / microtubule-based process / protein-disulfide reductase activity / microtubule / centrosome / ATP hydrolysis activity / ATP binding / cytoplasm 類似検索 - 分子機能 Kelch motif / : / Galactose oxidase, central domain / Dynein light chain Tctex-1 like / Tctex-1-like superfamily / Tctex-1 family / : / Dynein light chain type 1 / Dynein light chain, type 1/2 / Dynein light chain superfamily ... Kelch motif / : / Galactose oxidase, central domain / Dynein light chain Tctex-1 like / Tctex-1-like superfamily / Tctex-1 family / : / Dynein light chain type 1 / Dynein light chain, type 1/2 / Dynein light chain superfamily / Dynein light chain type 1 / Dynein heavy chain, AAA 5 extension domain / Dynein heavy chain AAA lid domain / Roadblock/LAMTOR2 domain / Roadblock/LC7 domain / Roadblock/LC7 domain / Dynein heavy chain 3, AAA+ lid domain / AAA+ lid domain / Dynein heavy chain, C-terminal domain / Dynein heavy chain, C-terminal domain, barrel region / Dynein heavy chain C-terminal domain / Filamin/ABP280 repeat / Filamin/ABP280 repeat profile. / Filamin/ABP280 repeat-like / P-loop containing dynein motor region / Dynein heavy chain, tail / Dynein heavy chain, N-terminal region 1 / Dynein heavy chain / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, linker / Dynein heavy chain, AAA module D4 / Dynein heavy chain, coiled coil stalk / Dynein heavy chain, hydrolytic ATP-binding dynein motor region / Dynein heavy chain, ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Dynein heavy chain AAA lid domain superfamily / Dynein heavy chain, domain 2, N-terminal / Dynein heavy chain, linker, subdomain 3 / Dynein heavy chain, AAA1 domain, small subdomain / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, N-terminal region 2 / Hydrolytic ATP binding site of dynein motor region / Microtubule-binding stalk of dynein motor / P-loop containing dynein motor region D4 / ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Thioredoxin / IPT/TIG domain / Kelch-type beta propeller / ig-like, plexins, transcription factors / Thioredoxin / IPT domain / Thioredoxin, conserved site / Thioredoxin family active site. / Thioredoxin domain profile. / Thioredoxin domain / EF-hand domain pair / Immunoglobulin E-set / Thioredoxin-like superfamily / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Immunoglobulin-like fold / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性 Dynein light chain tctex-type 1 protein / Dynein intermediate chain 2 / EF hand protein / Dynein-1-alpha heavy chain, flagellar inner arm I1 complex protein, putative / Outer arm dynein beta heavy chain / Dynein light chain roadblock-type 2 protein / Dynein light chain / Dynein light chain / Dynein light chain / Dynein light chain ... Dynein light chain tctex-type 1 protein / Dynein intermediate chain 2 / EF hand protein / Dynein-1-alpha heavy chain, flagellar inner arm I1 complex protein, putative / Outer arm dynein beta heavy chain / Dynein light chain roadblock-type 2 protein / Dynein light chain / Dynein light chain / Dynein light chain / Dynein light chain / Thioredoxin / Dynein light chain 2A / Dynein heavy chain, outer arm protein / Dynein light chain roadblock-type 2 protein / Dynein light chain / Flagellar outer dynein arm intermediate protein, putative / Dynein light chain 類似検索 - 構成要素生物種 Chlamydomonas reinhardtii (クラミドモナス)手法 サブトモグラム平均法 / クライオ電子顕微鏡法 / 解像度 : 38.0 Å 詳細 データ登録者Zimmermann NEL / Noga A / Obbineni JM / Ishikawa T 資金援助 スイス, 2件 詳細 詳細を隠すOrganization Grant number 国 Swiss National Science Foundation NF310030_192644 スイス Swiss National Science Foundation スイス
引用ジャーナル : EMBO J / 年 : 2023タイトル : ATP-induced conformational change of axonemal outer dynein arms revealed by cryo-electron tomography.著者 : Noemi Zimmermann / Akira Noga / Jagan Mohan Obbineni / Takashi Ishikawa / 要旨 : Axonemal outer dynein arm (ODA) motors generate force for ciliary beating. We analyzed three states of the ODA during the power stroke cycle using in situ cryo-electron tomography, subtomogram ... Axonemal outer dynein arm (ODA) motors generate force for ciliary beating. We analyzed three states of the ODA during the power stroke cycle using in situ cryo-electron tomography, subtomogram averaging, and classification. These states of force generation depict the prepower stroke, postpower stroke, and intermediate state conformations. Comparison of these conformations to published in vitro atomic structures of cytoplasmic dynein, ODA, and the Shulin-ODA complex revealed differences in the orientation and position of the dynein head. Our analysis shows that in the absence of ATP, all dynein linkers interact with the AAA3/AAA4 domains, indicating that interactions with the adjacent microtubule doublet B-tubule direct dynein orientation. For the prepower stroke conformation, there were changes in the tail that is anchored on the A-tubule. We built models starting with available high-resolution structures to generate a best-fitting model structure for the in situ pre- and postpower stroke ODA conformations, thereby showing that ODA in a complex with Shulin adopts a similar conformation as the active prepower stroke ODA in the axoneme. 履歴 登録 2022年12月7日 - ヘッダ(付随情報) 公開 2023年5月10日 - マップ公開 2023年5月10日 - 更新 2024年7月24日 - 現状 2024年7月24日 処理サイト : PDBe / 状態 : 公開
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