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基本情報
登録情報 | ![]() | |||||||||
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タイトル | Human TRiC-tubulin-S3 | |||||||||
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![]() | STRUCTURAL PROTEIN | |||||||||
機能・相同性 | ![]() odontoblast differentiation / positive regulation of establishment of protein localization to telomere / zona pellucida receptor complex / cytoskeleton-dependent intracellular transport / positive regulation of protein localization to Cajal body / scaRNA localization to Cajal body / positive regulation of telomerase RNA localization to Cajal body / tubulin complex assembly / chaperonin-containing T-complex / : ...odontoblast differentiation / positive regulation of establishment of protein localization to telomere / zona pellucida receptor complex / cytoskeleton-dependent intracellular transport / positive regulation of protein localization to Cajal body / scaRNA localization to Cajal body / positive regulation of telomerase RNA localization to Cajal body / tubulin complex assembly / chaperonin-containing T-complex / : / BBSome-mediated cargo-targeting to cilium / Formation of tubulin folding intermediates by CCT/TriC / Folding of actin by CCT/TriC / binding of sperm to zona pellucida / Prefoldin mediated transfer of substrate to CCT/TriC / GTPase activating protein binding / RHOBTB1 GTPase cycle / WD40-repeat domain binding / natural killer cell mediated cytotoxicity / pericentriolar material / regulation of synapse organization / nuclear envelope lumen / beta-tubulin binding / MHC class I protein binding / Association of TriC/CCT with target proteins during biosynthesis / chaperone-mediated protein complex assembly / microtubule-based process / heterochromatin / RHOBTB2 GTPase cycle / intercellular bridge / spindle assembly / : / positive regulation of telomere maintenance via telomerase / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / Recruitment of mitotic centrosome proteins and complexes / protein folding chaperone / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / Recruitment of NuMA to mitotic centrosomes / Anchoring of the basal body to the plasma membrane / acrosomal vesicle / AURKA Activation by TPX2 / mRNA 3'-UTR binding / cell projection / ATP-dependent protein folding chaperone / response to virus / structural constituent of cytoskeleton / microtubule cytoskeleton organization / mRNA 5'-UTR binding / cytoplasmic ribonucleoprotein granule / mitotic spindle / azurophil granule lumen / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / Regulation of PLK1 Activity at G2/M Transition / unfolded protein binding / melanosome / G-protein beta-subunit binding / protein folding / mitotic cell cycle / microtubule cytoskeleton / cell body / secretory granule lumen / microtubule / Potential therapeutics for SARS / ficolin-1-rich granule lumen / cytoskeleton / protein stabilization / cilium / cadherin binding / protein domain specific binding / membrane raft / cell division / GTPase activity / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / protein-containing complex binding / GTP binding / structural molecule activity / Golgi apparatus / protein-containing complex / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / metal ion binding / identical protein binding / nucleus / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
生物種 | ![]() | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.1 Å | |||||||||
![]() | Cong Y / Liu CX | |||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Pathway and mechanism of tubulin folding mediated by TRiC/CCT along its ATPase cycle revealed using cryo-EM. 著者: Caixuan Liu / Mingliang Jin / Shutian Wang / Wenyu Han / Qiaoyu Zhao / Yifan Wang / Cong Xu / Lei Diao / Yue Yin / Chao Peng / Lan Bao / Yanxing Wang / Yao Cong / ![]() 要旨: The eukaryotic chaperonin TRiC/CCT assists the folding of about 10% of cytosolic proteins through an ATP-driven conformational cycle, and the essential cytoskeleton protein tubulin is the obligate ...The eukaryotic chaperonin TRiC/CCT assists the folding of about 10% of cytosolic proteins through an ATP-driven conformational cycle, and the essential cytoskeleton protein tubulin is the obligate substrate of TRiC. Here, we present an ensemble of cryo-EM structures of endogenous human TRiC throughout its ATPase cycle, with three of them revealing endogenously engaged tubulin in different folding stages. The open-state TRiC-tubulin-S1 and -S2 maps show extra density corresponding to tubulin in the cis-ring chamber of TRiC. Our structural and XL-MS analyses suggest a gradual upward translocation and stabilization of tubulin within the TRiC chamber accompanying TRiC ring closure. In the closed TRiC-tubulin-S3 map, we capture a near-natively folded tubulin-with the tubulin engaging through its N and C domains mainly with the A and I domains of the CCT3/6/8 subunits through electrostatic and hydrophilic interactions. Moreover, we also show the potential role of TRiC C-terminal tails in substrate stabilization and folding. Our study delineates the pathway and molecular mechanism of TRiC-mediated folding of tubulin along the ATPase cycle of TRiC, and may also inform the design of therapeutic agents targeting TRiC-tubulin interactions. | |||||||||
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マップデータ | ![]() | 8.7 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 23.6 KB 23.6 KB | 表示 表示 | ![]() |
画像 | ![]() | 109.8 KB | ||
Filedesc metadata | ![]() | 8.8 KB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 7x0sMC ![]() 7wz3C ![]() 7x0aC ![]() 7x0vC ![]() 7x3jC ![]() 7x3uC ![]() 7x6qC ![]() 7x7yC M: このマップから作成された原子モデル C: 同じ文献を引用 ( |
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類似構造データ | 類似検索 - 機能・相同性 ![]() |
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「今月の分子」の関連する項目 |
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マップ
ファイル | ![]() | ||||||||||||||||||||||||||||||||||||
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投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.318 Å | ||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
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試料の構成要素
+全体 : Human TRiC-tubulin-S3
+超分子 #1: Human TRiC-tubulin-S3
+分子 #1: T-complex protein 1 subunit zeta
+分子 #2: T-complex protein 1 subunit theta
+分子 #3: T-complex protein 1 subunit eta
+分子 #4: T-complex protein 1 subunit gamma
+分子 #5: T-complex protein 1 subunit epsilon
+分子 #6: T-complex protein 1 subunit delta
+分子 #7: T-complex protein 1 subunit beta
+分子 #8: T-complex protein 1 subunit alpha
+分子 #9: Tubulin beta chain
+分子 #10: ADENOSINE-5'-DIPHOSPHATE
+分子 #11: MAGNESIUM ION
+分子 #12: ALUMINUM FLUORIDE
+分子 #13: water
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.5 / 構成要素 - 濃度: 50.0 mM / 構成要素 - 式: NaCl / 構成要素 - 名称: sodium Chloride |
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凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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撮影 | フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 検出モード: SUPER-RESOLUTION / 平均電子線量: 38.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 2.5 µm / 最小 デフォーカス(公称値): 0.8 µm |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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画像解析
初期モデル | モデルのタイプ: OTHER |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 3.1 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 103406 |
初期 角度割当 | タイプ: MAXIMUM LIKELIHOOD |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD |