+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-32823 | |||||||||
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タイトル | Prefoldin-tubulin-TRiC complex | |||||||||
マップデータ | A differently local sharpened main map for the refinement | |||||||||
試料 |
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キーワード | chapronin complex / CHAPERONE | |||||||||
機能・相同性 | 機能・相同性情報 RNA polymerase I assembly / RNA polymerase III assembly / prefoldin complex / positive regulation of cytoskeleton organization / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / RNA polymerase II core complex assembly ...RNA polymerase I assembly / RNA polymerase III assembly / prefoldin complex / positive regulation of cytoskeleton organization / zona pellucida receptor complex / scaRNA localization to Cajal body / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / RNA polymerase II core complex assembly / tubulin complex assembly / BBSome-mediated cargo-targeting to cilium / chaperonin-containing T-complex / RPAP3/R2TP/prefoldin-like complex / 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 / Prefoldin mediated transfer of substrate to CCT/TriC / negative regulation of amyloid fibril formation / protein folding chaperone complex / RHOBTB1 GTPase cycle / intermediate filament cytoskeleton / WD40-repeat domain binding / pericentriolar material / beta-tubulin binding / : / Association of TriC/CCT with target proteins during biosynthesis / microtubule-based process / chaperone-mediated protein complex assembly / RHOBTB2 GTPase cycle / heterochromatin / chaperone-mediated protein folding / protein folding chaperone / positive regulation of telomere maintenance via telomerase / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / tubulin binding / acrosomal vesicle / cell projection / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / response to virus / negative regulation of canonical Wnt signaling pathway / cilium / mRNA 5'-UTR binding / transcription corepressor activity / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / azurophil granule lumen / G-protein beta-subunit binding / unfolded protein binding / melanosome / protein folding / protein-folding chaperone binding / retina development in camera-type eye / amyloid-beta binding / cell body / secretory granule lumen / ficolin-1-rich granule lumen / microtubule / cytoskeleton / protein stabilization / cadherin binding / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / regulation of DNA-templated transcription / Golgi apparatus / ATP hydrolysis activity / mitochondrion / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||
生物種 | Homo sapiens (ヒト) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.85 Å | |||||||||
データ登録者 | Roh SH / Park J | |||||||||
資金援助 | 韓国, 1件
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引用 | ジャーナル: Cell / 年: 2022 タイトル: Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT. 著者: Daniel Gestaut / Yanyan Zhao / Junsun Park / Boxue Ma / Alexander Leitner / Miranda Collier / Grigore Pintilie / Soung-Hun Roh / Wah Chiu / Judith Frydman / 要旨: The ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis. To uncover why some eukaryotic proteins can only fold with TRiC assistance, we reconstituted the folding of ...The ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis. To uncover why some eukaryotic proteins can only fold with TRiC assistance, we reconstituted the folding of β-tubulin using human prefoldin and TRiC. We find unstructured β-tubulin is delivered by prefoldin to the open TRiC chamber followed by ATP-dependent chamber closure. Cryo-EM resolves four near-atomic-resolution structures containing progressively folded β-tubulin intermediates within the closed TRiC chamber, culminating in native tubulin. This substrate folding pathway appears closely guided by site-specific interactions with conserved regions in the TRiC chamber. Initial electrostatic interactions between the TRiC interior wall and both the folded tubulin N domain and its C-terminal E-hook tail establish the native substrate topology, thus enabling C-domain folding. Intrinsically disordered CCT C termini within the chamber promote subsequent folding of tubulin's core and middle domains and GTP-binding. Thus, TRiC's chamber provides chemical and topological directives that shape the folding landscape of its obligate substrates. | |||||||||
履歴 |
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-構造の表示
添付画像 |
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-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_32823.map.gz | 118 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-32823-v30.xml emd-32823.xml | 38 KB 38 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_32823_fsc.xml | 11.1 KB | 表示 | FSCデータファイル |
画像 | emd_32823.png | 87.7 KB | ||
Filedesc metadata | emd-32823.cif.gz | 10.2 KB | ||
その他 | emd_32823_additional_1.map.gz emd_32823_half_map_1.map.gz emd_32823_half_map_2.map.gz | 118 MB 115.9 MB 115.9 MB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-32823 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-32823 | HTTPS FTP |
-関連構造データ
-リンク
EMDBのページ | EMDB (EBI/PDBe) / EMDataResource |
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「今月の分子」の関連する項目 |
-マップ
ファイル | ダウンロード / ファイル: emd_32823.map.gz / 形式: CCP4 / 大きさ: 125 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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注釈 | A differently local sharpened main map for the refinement | ||||||||||||||||||||||||||||||||||||
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: 1.02 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
-追加マップ: A B-factor sharpened map
ファイル | emd_32823_additional_1.map | ||||||||||||
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注釈 | A B-factor sharpened map | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: A half map
ファイル | emd_32823_half_map_1.map | ||||||||||||
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注釈 | A half map | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: A half map
ファイル | emd_32823_half_map_2.map | ||||||||||||
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注釈 | A half map | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-試料の構成要素
+全体 : Ternary complex of TRiC/CCT, beta-tubulin, prefoldin complex
+超分子 #1: Ternary complex of TRiC/CCT, beta-tubulin, prefoldin complex
+分子 #1: Prefoldin subunit 1
+分子 #2: Prefoldin subunit 2
+分子 #3: Prefoldin subunit 3
+分子 #4: Prefoldin subunit 4
+分子 #5: Prefoldin subunit 5
+分子 #6: Prefoldin subunit 6
+分子 #7: T-complex protein 1 subunit alpha
+分子 #8: T-complex protein 1 subunit beta
+分子 #9: T-complex protein 1 subunit gamma
+分子 #10: T-complex protein 1 subunit delta
+分子 #11: T-complex protein 1 subunit epsilon
+分子 #12: T-complex protein 1 subunit zeta
+分子 #13: T-complex protein 1 subunit eta
+分子 #14: T-complex protein 1 subunit theta
+分子 #15: ADENOSINE-5'-DIPHOSPHATE
-実験情報
-構造解析
手法 | クライオ電子顕微鏡法 |
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解析 | 単粒子再構成法 |
試料の集合状態 | 3D array |
-試料調製
緩衝液 | pH: 7.4 構成要素:
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グリッド | モデル: Quantifoil R1.2/1.3 / 材質: COPPER / 支持フィルム - 材質: CARBON / 支持フィルム - トポロジー: HOLEY / 前処理 - タイプ: GLOW DISCHARGE | |||||||||
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / 装置: FEI VITROBOT MARK IV |
-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: COUNTING / 実像数: 11796 / 平均電子線量: 50.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: FIELD EMISSION GUN |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm / 最大 デフォーカス(公称値): 3.5 µm / 最小 デフォーカス(公称値): 0.5 µm |
試料ステージ | 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER ホルダー冷却材: NITROGEN |
実験機器 | モデル: Titan Krios / 画像提供: FEI Company |