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基本情報
登録情報 | データベース: PDB / ID: 7nvm | |||||||||
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タイトル | Human TRiC complex in closed state with nanobody Nb18, actin and PhLP2A bound | |||||||||
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![]() | CHAPERONE / TRiC / CCT / ATP hydrolysis / type II chaperonin / protein folding / actin / Structural Genomics / Structural Genomics Consortium / SGC | |||||||||
機能・相同性 | ![]() basal body patch / negative regulation of chaperone-mediated protein folding / perinucleolar compartment / tight junction assembly / regulation of transepithelial transport / morphogenesis of a polarized epithelium / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / structural constituent of postsynaptic actin cytoskeleton ...basal body patch / negative regulation of chaperone-mediated protein folding / perinucleolar compartment / tight junction assembly / regulation of transepithelial transport / morphogenesis of a polarized epithelium / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / structural constituent of postsynaptic actin cytoskeleton / profilin binding / positive regulation of establishment of protein localization to telomere / protein localization to bicellular tight junction / positive regulation of protein localization to Cajal body / tubulin complex assembly / BBSome-mediated cargo-targeting to cilium / dense body / Formation of annular gap junctions / Gap junction degradation / Cell-extracellular matrix interactions / Folding of actin by CCT/TriC / binding of sperm to zona pellucida / Formation of tubulin folding intermediates by CCT/TriC / positive regulation of telomerase RNA localization to Cajal body / vascular endothelial growth factor receptor 2 binding / Prefoldin mediated transfer of substrate to CCT/TriC / chaperonin-containing T-complex / Adherens junctions interactions / regulation of stress fiber assembly / Sensory processing of sound by outer hair cells of the cochlea / Interaction between L1 and Ankyrins / Sensory processing of sound by inner hair cells of the cochlea / RHOBTB1 GTPase cycle / regulation of synaptic vesicle endocytosis / intermediate filament cytoskeleton / WD40-repeat domain binding / apical junction complex / regulation of focal adhesion assembly / positive regulation of wound healing / maintenance of blood-brain barrier / myofibril / sarcomere organization / NuA4 histone acetyltransferase complex / pericentriolar material / beta-tubulin binding / Recycling pathway of L1 / Association of TriC/CCT with target proteins during biosynthesis / filamentous actin / calyx of Held / chaperone-mediated protein complex assembly / EPH-ephrin mediated repulsion of cells / RHO GTPases Activate WASPs and WAVEs / RHO GTPases activate IQGAPs / RHOBTB2 GTPase cycle / heterochromatin / chaperone-mediated protein folding / regulation of peptidyl-tyrosine phosphorylation / protein folding chaperone / positive regulation of telomerase activity / positive regulation of endothelial cell proliferation / positive regulation of telomere maintenance via telomerase / EPHB-mediated forward signaling / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / phagocytic vesicle / negative regulation of ubiquitin-dependent protein catabolic process / axonogenesis / acrosomal vesicle / mRNA 3'-UTR binding / cell projection / Translocation of SLC2A4 (GLUT4) to the plasma membrane / RHO GTPases Activate Formins / cell motility / actin filament / FCGR3A-mediated phagocytosis / ATP-dependent protein folding chaperone / 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 / Signaling by high-kinase activity BRAF mutants / Schaffer collateral - CA1 synapse / response to virus / MAP2K and MAPK activation / structural constituent of cytoskeleton / Regulation of actin dynamics for phagocytic cup formation / mRNA 5'-UTR binding / cilium / platelet aggregation / VEGFA-VEGFR2 Pathway / cellular response to type II interferon / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / positive regulation of angiogenesis / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / G-protein beta-subunit binding / azurophil granule lumen / Signaling by BRAF and RAF1 fusions / cell-cell junction / unfolded protein binding / melanosome / protein folding 類似検索 - 分子機能 | |||||||||
生物種 | ![]() ![]() ![]() | |||||||||
手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.1 Å | |||||||||
![]() | Kelly, J.J. / Chi, G. / Bulawa, C. / Paavilainen, V.O. / Bountra, C. / Huiskonen, J.T. / Yue, W. / Structural Genomics Consortium (SGC) | |||||||||
資金援助 | ![]() ![]()
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![]() | ![]() タイトル: Snapshots of actin and tubulin folding inside the TRiC chaperonin. 著者: John J Kelly / Dale Tranter / Els Pardon / Gamma Chi / Holger Kramer / Lotta Happonen / Kelly M Knee / Jay M Janz / Jan Steyaert / Christine Bulawa / Ville O Paavilainen / Juha T Huiskonen / Wyatt W Yue / ![]() ![]() ![]() ![]() ![]() 要旨: The integrity of a cell's proteome depends on correct folding of polypeptides by chaperonins. The chaperonin TCP-1 ring complex (TRiC) acts as obligate folder for >10% of cytosolic proteins, ...The integrity of a cell's proteome depends on correct folding of polypeptides by chaperonins. The chaperonin TCP-1 ring complex (TRiC) acts as obligate folder for >10% of cytosolic proteins, including he cytoskeletal proteins actin and tubulin. Although its architecture and how it recognizes folding substrates are emerging from structural studies, the subsequent fate of substrates inside the TRiC chamber is not defined. We trapped endogenous human TRiC with substrates (actin, tubulin) and cochaperone (PhLP2A) at different folding stages, for structure determination by cryo-EM. The already-folded regions of client proteins are anchored at the chamber wall, positioning unstructured regions toward the central space to achieve their native fold. Substrates engage with different sections of the chamber during the folding cycle, coupled to TRiC open-and-close transitions. Further, the cochaperone PhLP2A modulates folding, acting as a molecular strut between substrate and TRiC chamber. Our structural snapshots piece together an emerging model of client protein folding within TRiC. | |||||||||
履歴 |
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構造の表示
ムービー |
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構造ビューア | 分子: ![]() ![]() |
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ダウンロードとリンク
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ダウンロード
PDBx/mmCIF形式 | ![]() | 1.5 MB | 表示 | ![]() |
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PDB形式 | ![]() | 1.3 MB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 2.2 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 2.2 MB | 表示 | |
XML形式データ | ![]() | 220.8 KB | 表示 | |
CIF形式データ | ![]() | 342.4 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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リンク
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集合体
登録構造単位 | ![]()
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要素
-T-complex protein 1 subunit ... , 8種, 16分子 AaBbDdEeGgHhQqZz
#1: タンパク質 | 分子量: 60418.477 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() #2: タンパク質 | 分子量: 57567.141 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() #3: タンパク質 | 分子量: 57996.113 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() #4: タンパク質 | 分子量: 59749.957 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #5: タンパク質 | 分子量: 60613.855 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() #6: タンパク質 | 分子量: 59443.535 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() #8: タンパク質 | 分子量: 59691.422 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() #9: タンパク質 | 分子量: 58106.086 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) ![]() |
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-タンパク質 , 2種, 2分子 KP
#10: タンパク質 | 分子量: 41838.766 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() |
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#11: タンパク質 | 分子量: 27650.383 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) ![]() |
-抗体 , 1種, 2分子 Nn
#7: 抗体 | 分子量: 14412.816 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() ![]() |
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-非ポリマー , 4種, 67分子 ![](data/chem/img/ADP.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/AF3.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/MG.gif)
![](data/chem/img/AF3.gif)
![](data/chem/img/HOH.gif)
#12: 化合物 | ChemComp-ADP / #13: 化合物 | ChemComp-MG / #14: 化合物 | ChemComp-AF3 / #15: 水 | ChemComp-HOH / | |
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-詳細
研究の焦点であるリガンドがあるか | N |
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-実験情報
-実験
実験 | 手法: 電子顕微鏡法 |
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EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
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試料調製
構成要素 |
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分子量 | 実験値: NO | ||||||||||||||||||||||||||||||
由来(天然) |
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由来(組換発現) |
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緩衝液 | pH: 7.5 | ||||||||||||||||||||||||||||||
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||||||||||||||
急速凍結 | 凍結剤: ETHANE |
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電子顕微鏡撮影
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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顕微鏡 | モデル: TFS KRIOS |
電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD |
撮影 | 電子線照射量: 43 e/Å2 フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
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解析
ソフトウェア |
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CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
対称性 | 点対称性: C1 (非対称) | ||||||||||||||||||||||||
3次元再構成 | 解像度: 3.1 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 63082 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
精密化 | 交差検証法: NONE 立体化学のターゲット値: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
原子変位パラメータ | Biso mean: 71.38 Å2 | ||||||||||||||||||||||||
拘束条件 |
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