- EMDB-20050: CryoEM focus classification map of the hyperactive ClpB mutant K4... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-20050
タイトル
CryoEM focus classification map of the hyperactive ClpB mutant K476C, bound to casein, post-state
マップデータ
EM focus classification map of the hyperactive ClpB mutant K476C, bound to casein, post-state
試料
複合体: hyperactive disaggregase ClpB K476C, bound to casein
タンパク質・ペプチド: Hyperactive disaggregase ClpB
リガンド: ADENOSINE-5'-DIPHOSPHATE
キーワード
disaggregase / CLPB / AAA+ / CHAPERONE (シャペロン)
機能・相同性
機能・相同性情報
protein unfolding / cellular response to heat / response to heat / protein refolding / ATP hydrolysis activity / ATP binding / 生体膜 / identical protein binding / 細胞質基質 / 細胞質 類似検索 - 分子機能
Chaperonin ClpB / ClpA/B, conserved site 2 / Chaperonins clpA/B signature 2. / ClpA/B, conserved site 1 / Chaperonins clpA/B signature 1. / ClpA/ClpB, AAA lid domain / AAA lid domain / Clp amino terminal domain, pathogenicity island component / Clp repeat (R) domain profile. / Clp, repeat (R) domain ...Chaperonin ClpB / ClpA/B, conserved site 2 / Chaperonins clpA/B signature 2. / ClpA/B, conserved site 1 / Chaperonins clpA/B signature 1. / ClpA/ClpB, AAA lid domain / AAA lid domain / Clp amino terminal domain, pathogenicity island component / Clp repeat (R) domain profile. / Clp, repeat (R) domain / Clp, N-terminal domain superfamily / ClpA/B family / Clp ATPase, C-terminal / AAA domain (Cdc48 subfamily) / C-terminal, D2-small domain, of ClpB protein / C-terminal, D2-small domain, of ClpB protein / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性
ジャーナル: Nat Commun / 年: 2019 タイトル: Structural basis for substrate gripping and translocation by the ClpB AAA+ disaggregase. 著者: Alexandrea N Rizo / JiaBei Lin / Stephanie N Gates / Eric Tse / Stephen M Bart / Laura M Castellano / Frank DiMaio / James Shorter / Daniel R Southworth / 要旨: Bacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases that serve critical functions in proteostasis by solubilizing protein aggregates. Two AAA+ nucleotide binding domains (NBDs) ...Bacterial ClpB and yeast Hsp104 are homologous Hsp100 protein disaggregases that serve critical functions in proteostasis by solubilizing protein aggregates. Two AAA+ nucleotide binding domains (NBDs) power polypeptide translocation through a central channel comprised of a hexameric spiral of protomers that contact substrate via conserved pore-loop interactions. Here we report cryo-EM structures of a hyperactive ClpB variant bound to the model substrate, casein in the presence of slowly hydrolysable ATPγS, which reveal the translocation mechanism. Distinct substrate-gripping interactions are identified for NBD1 and NBD2 pore loops. A trimer of N-terminal domains define a channel entrance that binds the polypeptide substrate adjacent to the topmost NBD1 contact. NBD conformations at the seam interface reveal how ATP hydrolysis-driven substrate disengagement and re-binding are precisely tuned to drive a directional, stepwise translocation cycle.