- EMDB-35199: The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in... -
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基本情報
登録情報
データベース: EMDB / ID: EMD-35199
タイトル
The focused refinement of CCT3-PhLP2A from TRiC-PhLP2A complex in the open state
マップデータ
試料
複合体: Complex of TRiC/CCT and PhLP2A
複合体: PhLP2A (PDCL3)
タンパク質・ペプチド: Phosducin-like protein 3
複合体: TRiC/CCT
タンパク質・ペプチド: T-complex protein 1 subunit gamma
リガンド: ADENOSINE-5'-DIPHOSPHATE
キーワード
chaperonin complex / CHAPERONE / cochaperone
機能・相同性
機能・相同性情報
negative regulation of chaperone-mediated protein folding / perinucleolar compartment / zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / chaperonin-containing T-complex / BBSome-mediated cargo-targeting to cilium / binding of sperm to zona pellucida / positive regulation of telomerase RNA localization to Cajal body / Folding of actin by CCT/TriC ...negative regulation of chaperone-mediated protein folding / perinucleolar compartment / zona pellucida receptor complex / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / chaperonin-containing T-complex / BBSome-mediated cargo-targeting to cilium / binding of sperm to zona pellucida / positive regulation of telomerase RNA localization to Cajal body / Folding of actin by CCT/TriC / Formation of tubulin folding intermediates by CCT/TriC / vascular endothelial growth factor receptor 2 binding / Prefoldin mediated transfer of substrate to CCT/TriC / Association of TriC/CCT with target proteins during biosynthesis / negative regulation of ubiquitin-dependent protein catabolic process / regulation of peptidyl-tyrosine phosphorylation / chaperone-mediated protein folding / protein folding chaperone / positive regulation of endothelial cell proliferation / positive regulation of telomere maintenance via telomerase / ATP-dependent protein folding chaperone / positive regulation of angiogenesis / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / unfolded protein binding / protein folding / cell body / actin cytoskeleton organization / angiogenesis / microtubule / cytoskeleton / protein stabilization / positive regulation of gene expression / apoptotic process / perinuclear region of cytoplasm / endoplasmic reticulum / ATP hydrolysis activity / protein-containing complex / RNA binding / extracellular exosome / nucleoplasm / ATP binding / cytosol / cytoplasm 類似検索 - 分子機能
ジャーナル: Nat Commun / 年: 2024 タイトル: A structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle. 著者: Junsun Park / Hyunmin Kim / Daniel Gestaut / Seyeon Lim / Kwadwo A Opoku-Nsiah / Alexander Leitner / Judith Frydman / Soung-Hun Roh / 要旨: Proper cellular proteostasis, essential for viability, requires a network of chaperones and cochaperones. ATP-dependent chaperonin TRiC/CCT partners with cochaperones prefoldin (PFD) and phosducin- ...Proper cellular proteostasis, essential for viability, requires a network of chaperones and cochaperones. ATP-dependent chaperonin TRiC/CCT partners with cochaperones prefoldin (PFD) and phosducin-like proteins (PhLPs) to facilitate folding of essential eukaryotic proteins. Using cryoEM and biochemical analyses, we determine the ATP-driven cycle of TRiC-PFD-PhLP2A interaction. PhLP2A binds to open apo-TRiC through polyvalent domain-specific contacts with its chamber's equatorial and apical regions. PhLP2A N-terminal H3-domain binding to subunits CCT3/4 apical domains displace PFD from TRiC. ATP-induced TRiC closure rearranges the contacts of PhLP2A domains within the closed chamber. In the presence of substrate, actin and PhLP2A segregate into opposing chambers, each binding to positively charged inner surface residues from CCT1/3/6/8. Notably, actin induces a conformational change in PhLP2A, causing its N-terminal helices to extend across the inter-ring interface to directly contact a hydrophobic groove in actin. Our findings reveal an ATP-driven PhLP2A structural rearrangement cycle within the TRiC chamber to facilitate folding.