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データを開く
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基本情報
登録情報 | データベース: EMDB / ID: EMD-0495 | ||||||||||||||||||||||||
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タイトル | hTRiC-hPFD Class4 | ||||||||||||||||||||||||
![]() | hTRiC-hPFD Class4 | ||||||||||||||||||||||||
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![]() | TRiC/CCT / PFD / CryoEM / Molecular Chaperone / Protein folding / CHAPERONE | ||||||||||||||||||||||||
機能・相同性 | ![]() RNA polymerase I assembly / RNA polymerase III assembly / prefoldin complex / positive regulation of cytoskeleton organization / zona pellucida receptor complex / positive regulation of protein localization to Cajal body / scaRNA localization to Cajal body / positive regulation of establishment of protein localization to telomere / RNA polymerase II core complex assembly / positive regulation of telomerase RNA localization to Cajal body ...RNA polymerase I assembly / RNA polymerase III assembly / prefoldin complex / positive regulation of cytoskeleton organization / zona pellucida receptor complex / positive regulation of protein localization to Cajal body / scaRNA localization to Cajal body / positive regulation of establishment of protein localization to telomere / RNA polymerase II core complex assembly / positive regulation of telomerase RNA localization to Cajal body / tubulin complex assembly / chaperonin-containing T-complex / : / BBSome-mediated cargo-targeting to cilium / RPAP3/R2TP/prefoldin-like complex / Folding of actin by CCT/TriC / Formation of tubulin folding intermediates by CCT/TriC / binding of sperm to zona pellucida / 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 / heterochromatin / chaperone-mediated protein complex assembly / microtubule-based process / RHOBTB2 GTPase cycle / : / positive regulation of telomere maintenance via telomerase / protein folding chaperone / tubulin binding / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / acrosomal vesicle / cell projection / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / negative regulation of canonical Wnt signaling pathway / response to virus / cilium / mRNA 5'-UTR binding / transcription corepressor activity / azurophil granule lumen / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / G-protein beta-subunit binding / unfolded protein binding / melanosome / protein folding / amyloid-beta binding / protein-folding chaperone binding / cell body / retina development in camera-type eye / secretory granule lumen / microtubule / ficolin-1-rich granule lumen / 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 / 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: 8.2 Å | ||||||||||||||||||||||||
![]() | Gestaut DR / Roh SH | ||||||||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: The Chaperonin TRiC/CCT Associates with Prefoldin through a Conserved Electrostatic Interface Essential for Cellular Proteostasis. 著者: Daniel Gestaut / Soung Hun Roh / Boxue Ma / Grigore Pintilie / Lukasz A Joachimiak / Alexander Leitner / Thomas Walzthoeni / Ruedi Aebersold / Wah Chiu / Judith Frydman / ![]() ![]() ![]() ![]() 要旨: Maintaining proteostasis in eukaryotic protein folding involves cooperation of distinct chaperone systems. To understand how the essential ring-shaped chaperonin TRiC/CCT cooperates with the ...Maintaining proteostasis in eukaryotic protein folding involves cooperation of distinct chaperone systems. To understand how the essential ring-shaped chaperonin TRiC/CCT cooperates with the chaperone prefoldin/GIMc (PFD), we integrate cryoelectron microscopy (cryo-EM), crosslinking-mass-spectrometry and biochemical and cellular approaches to elucidate the structural and functional interplay between TRiC/CCT and PFD. We find these hetero-oligomeric chaperones associate in a defined architecture, through a conserved interface of electrostatic contacts that serves as a pivot point for a TRiC-PFD conformational cycle. PFD alternates between an open "latched" conformation and a closed "engaged" conformation that aligns the PFD-TRiC substrate binding chambers. PFD can act after TRiC bound its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles. Disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates. The supra-chaperone assembly formed by PFD and TRiC is essential to prevent toxic conformations and ensure effective cellular proteostasis. | ||||||||||||||||||||||||
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 | EMマップ: ![]() ![]() ![]() |
添付画像 |
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ダウンロードとリンク
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マップデータ | ![]() | 48.9 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 38.9 KB 38.9 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 8.7 KB | 表示 | ![]() |
画像 | ![]() | 117 KB | ||
Filedesc metadata | ![]() | 9.3 KB | ||
その他 | ![]() ![]() ![]() | 40.8 MB 40.9 MB 40.9 MB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 992.2 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 991.8 KB | 表示 | |
XML形式データ | ![]() | 14.3 KB | 表示 | |
CIF形式データ | ![]() | 20.3 KB | 表示 | |
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 | ![]() 6nrdMC ![]() 0490C ![]() 0491C ![]() 0492C ![]() 0493C ![]() 0494C ![]() 0496C ![]() 6nr8C ![]() 6nr9C ![]() 6nraC ![]() 6nrbC ![]() 6nrcC C: 同じ文献を引用 ( M: このマップから作成された原子モデル |
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リンク
EMDBのページ | ![]() ![]() |
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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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注釈 | hTRiC-hPFD Class4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 1.7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
CCP4マップ ヘッダ情報:
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-添付データ
-追加マップ: hTRiC-hPFD Class4, unfiltered sum map
ファイル | emd_0495_additional.map | ||||||||||||
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注釈 | hTRiC-hPFD Class4, unfiltered sum 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: hTRiC-hPFD Class4, half map 1
ファイル | emd_0495_half_map_1.map | ||||||||||||
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注釈 | hTRiC-hPFD Class4, half map 1 | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: hTRiC-hPFD Class4, half map 2
ファイル | emd_0495_half_map_2.map | ||||||||||||
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注釈 | hTRiC-hPFD Class4, half map 2 | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
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試料の構成要素
+全体 : hTRiC-hPFD
+超分子 #1: hTRiC-hPFD
+超分子 #2: hTRiC
+超分子 #3: hPFD
+分子 #1: T-complex protein 1 subunit alpha
+分子 #2: T-complex protein 1 subunit beta
+分子 #3: T-complex protein 1 subunit gamma
+分子 #4: T-complex protein 1 subunit delta
+分子 #5: T-complex protein 1 subunit epsilon
+分子 #6: T-complex protein 1 subunit zeta
+分子 #7: T-complex protein 1 subunit eta
+分子 #8: T-complex protein 1 subunit theta
+分子 #9: Prefoldin subunit 1
+分子 #10: Prefoldin subunit 2
+分子 #11: Prefoldin subunit 3
+分子 #12: Prefoldin subunit 4
+分子 #13: Prefoldin subunit 5
+分子 #14: Prefoldin subunit 6
-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 |
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グリッド | 詳細: unspecified |
凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
顕微鏡 | JEOL 3200FSC |
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撮影 | フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) 平均電子線量: 48.0 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 |