- EMDB-33920: yeast TRiC-plp2-actin complex at S4 closed TRiC state -
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基本情報
登録情報
データベース: EMDB / ID: EMD-33920
タイトル
yeast TRiC-plp2-actin complex at S4 closed TRiC state
マップデータ
試料
複合体: yeast TRiC-plp2-actin complex at C4 closed TRiC state
複合体: TRiC
タンパク質・ペプチド: x 8種
複合体: plp2
タンパク質・ペプチド: x 1種
リガンド: x 4種
キーワード
TRiC/CCT / actin / phosducin-like protein / CHAPERONE
機能・相同性
機能・相同性情報
negative regulation of chaperone-mediated protein folding / Association of TriC/CCT with target proteins during biosynthesis / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / response to pheromone / chaperone mediated protein folding independent of cofactor / vascular endothelial growth factor receptor 2 binding / chaperonin-containing T-complex / negative regulation of signal transduction / protein folding chaperone / Neutrophil degranulation ...negative regulation of chaperone-mediated protein folding / Association of TriC/CCT with target proteins during biosynthesis / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / response to pheromone / chaperone mediated protein folding independent of cofactor / vascular endothelial growth factor receptor 2 binding / chaperonin-containing T-complex / negative regulation of signal transduction / protein folding chaperone / Neutrophil degranulation / ATP-dependent protein folding chaperone / G-protein beta/gamma-subunit complex binding / unfolded protein binding / protein folding / actin binding / actin cytoskeleton organization / regulation of cell cycle / positive regulation of gene expression / ATP hydrolysis activity / positive regulation of transcription by RNA polymerase II / ATP binding / plasma membrane / cytoplasm 類似検索 - 分子機能
T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / Chaperonins TCP-1 signature 1. / Chaperonins TCP-1 signature 2. ...T-complex protein 1, alpha subunit / T-complex protein 1, eta subunit / T-complex protein 1, theta subunit / T-complex protein 1, zeta subunit / T-complex protein 1, delta subunit / T-complex protein 1, gamma subunit / T-complex protein 1, epsilon subunit / T-complex protein 1, beta subunit / Chaperonins TCP-1 signature 1. / Chaperonins TCP-1 signature 2. / Chaperonin TCP-1, conserved site / Chaperonins TCP-1 signature 3. / Chaperone tailless complex polypeptide 1 (TCP-1) / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family / Thioredoxin-like superfamily 類似検索 - ドメイン・相同性
T-complex protein 1 subunit alpha / T-complex protein 1 subunit beta / T-complex protein 1 subunit gamma / T-complex protein 1 subunit delta / T-complex protein 1 subunit zeta / T-complex protein 1 subunit epsilon / T-complex protein 1 subunit eta / T-complex protein 1 subunit theta / Phosducin-like protein 2 類似検索 - 構成要素
ジャーナル: Sci Adv / 年: 2023 タイトル: Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT. 著者: Wenyu Han / Mingliang Jin / Caixuan Liu / Qiaoyu Zhao / Shutian Wang / Yifan Wang / Yue Yin / Chao Peng / Yanxing Wang / Yao Cong / 要旨: The cytoskeletal proteins tubulin and actin are the obligate substrates of TCP-1 ring complex/Chaperonin containing TCP-1 (TRiC/CCT), and their folding involves co-chaperone. Through cryo-electron ...The cytoskeletal proteins tubulin and actin are the obligate substrates of TCP-1 ring complex/Chaperonin containing TCP-1 (TRiC/CCT), and their folding involves co-chaperone. Through cryo-electron microscopy analysis, we present a more complete picture of TRiC-assisted tubulin/actin folding along TRiC adenosine triphosphatase cycle, under the coordination of co-chaperone plp2. In the open S1/S2 states, plp2 and tubulin/actin engaged within opposite TRiC chambers. Notably, we captured an unprecedented TRiC-plp2-tubulin complex in the closed S3 state, engaged with a folded full-length -tubulin and loaded with a guanosine triphosphate, and a plp2 occupying opposite rings. Another closed S4 state revealed an actin in the intermediate folding state and a plp2. Accompanying TRiC ring closure, plp2 translocation could coordinate substrate translocation on the CCT6 hemisphere, facilitating substrate stabilization and folding. Our findings reveal the folding mechanism of the major cytoskeletal proteins tubulin/actin under the coordination of the biogenesis machinery TRiC and plp2 and extend our understanding of the links between cytoskeletal proteostasis and related human diseases.