+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-23526 | |||||||||||||||||||||||||||||||||
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タイトル | Human TRiC/CCT complex with reovirus outer capsid protein sigma-3 | |||||||||||||||||||||||||||||||||
マップデータ | ||||||||||||||||||||||||||||||||||
試料 |
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キーワード | tric / cct / reovirus capsid / sigma 3 / CHAPERONE | |||||||||||||||||||||||||||||||||
機能・相同性 | 機能・相同性情報 zona pellucida receptor complex / scaRNA localization to Cajal body / symbiont-mediated suppression of host PKR/eIFalpha signaling / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / viral outer capsid / tubulin complex assembly / BBSome-mediated cargo-targeting to cilium / chaperonin-containing T-complex ...zona pellucida receptor complex / scaRNA localization to Cajal body / symbiont-mediated suppression of host PKR/eIFalpha signaling / chaperone mediated protein folding independent of cofactor / positive regulation of establishment of protein localization to telomere / positive regulation of protein localization to Cajal body / viral outer capsid / tubulin complex assembly / BBSome-mediated cargo-targeting to cilium / chaperonin-containing T-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 / protein serine/threonine kinase inhibitor activity / RHOBTB1 GTPase cycle / intermediate filament cytoskeleton / WD40-repeat domain binding / pericentriolar material / beta-tubulin binding / : / Association of TriC/CCT with target proteins during biosynthesis / chaperone-mediated protein complex assembly / RHOBTB2 GTPase cycle / heterochromatin / chaperone-mediated protein folding / protein folding chaperone / positive regulation of telomere maintenance via telomerase / viral life cycle / 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 / response to virus / cilium / mRNA 5'-UTR binding / 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 / regulation of translation / cell body / secretory granule lumen / ficolin-1-rich granule lumen / host cell cytoplasm / microtubule / cytoskeleton / protein stabilization / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont-mediated suppression of host innate immune response / cadherin binding / virus-mediated perturbation of host defense response / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / host cell nucleus / structural molecule activity / Golgi apparatus / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / metal ion binding / cytosol / cytoplasm 類似検索 - 分子機能 | |||||||||||||||||||||||||||||||||
生物種 | Homo sapiens (ヒト) / Mammalian orthoreovirus 3 Dearing (ウイルス) / Reovirus type 3 (strain Dearing) (ウイルス) | |||||||||||||||||||||||||||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 6.2 Å | |||||||||||||||||||||||||||||||||
データ登録者 | Knowlton JJ / Gestaut D / Ma B / Taylor G / Seven AB / Leitner A / Wilson GJ / Shanker S / Yates NA / Prasad BVV ...Knowlton JJ / Gestaut D / Ma B / Taylor G / Seven AB / Leitner A / Wilson GJ / Shanker S / Yates NA / Prasad BVV / Aebersold R / Chiu W / Frydman J / Dermody TS | |||||||||||||||||||||||||||||||||
資金援助 | 米国, European Union, 10件
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引用 | ジャーナル: Proc Natl Acad Sci U S A / 年: 2021 タイトル: Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network. 著者: Jonathan J Knowlton / Daniel Gestaut / Boxue Ma / Gwen Taylor / Alpay Burak Seven / Alexander Leitner / Gregory J Wilson / Sreejesh Shanker / Nathan A Yates / B V Venkataram Prasad / Ruedi ...著者: Jonathan J Knowlton / Daniel Gestaut / Boxue Ma / Gwen Taylor / Alpay Burak Seven / Alexander Leitner / Gregory J Wilson / Sreejesh Shanker / Nathan A Yates / B V Venkataram Prasad / Ruedi Aebersold / Wah Chiu / Judith Frydman / Terence S Dermody / 要旨: Intracellular protein homeostasis is maintained by a network of chaperones that function to fold proteins into their native conformation. The eukaryotic TRiC chaperonin (TCP1-ring complex, also ...Intracellular protein homeostasis is maintained by a network of chaperones that function to fold proteins into their native conformation. The eukaryotic TRiC chaperonin (TCP1-ring complex, also called CCT for cytosolic chaperonin containing TCP1) facilitates folding of a subset of proteins with folding constraints such as complex topologies. To better understand the mechanism of TRiC folding, we investigated the biogenesis of an obligate TRiC substrate, the reovirus σ3 capsid protein. We discovered that the σ3 protein interacts with a network of chaperones, including TRiC and prefoldin. Using a combination of cryoelectron microscopy, cross-linking mass spectrometry, and biochemical approaches, we establish functions for TRiC and prefoldin in folding σ3 and promoting its assembly into higher-order oligomers. These studies illuminate the molecular dynamics of σ3 folding and establish a biological function for TRiC in virus assembly. In addition, our findings provide structural and functional insight into the mechanism by which TRiC and prefoldin participate in the assembly of protein complexes. | |||||||||||||||||||||||||||||||||
履歴 |
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-構造の表示
ムービー |
ムービービューア |
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構造ビューア | EMマップ: SurfViewMolmilJmol/JSmol |
添付画像 |
-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_23526.map.gz | 77.1 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-23526-v30.xml emd-23526.xml | 28.3 KB 28.3 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_23526.png | 233 KB | ||
Filedesc metadata | emd-23526.cif.gz | 9.1 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-23526 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-23526 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_23526_validation.pdf.gz | 600.5 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_23526_full_validation.pdf.gz | 600 KB | 表示 | |
XML形式データ | emd_23526_validation.xml.gz | 6.1 KB | 表示 | |
CIF形式データ | emd_23526_validation.cif.gz | 6.9 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-23526 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-23526 | 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_23526.map.gz / 形式: CCP4 / 大きさ: 83.7 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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: 1.3 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
-試料の構成要素
+全体 : human TRiC/CCT complex with reovirus outer capsid protein sigma-3
+超分子 #1: human TRiC/CCT complex with reovirus outer capsid protein sigma-3
+超分子 #2: human TRiC/CCT complex
+超分子 #3: reovirus outer capsid protein sigma-3
+分子 #1: T-complex protein 1 subunit epsilon
+分子 #2: T-complex protein 1 subunit beta
+分子 #3: T-complex protein 1 subunit delta
+分子 #4: T-complex protein 1 subunit gamma
+分子 #5: T-complex protein 1 subunit eta
+分子 #6: T-complex protein 1 subunit theta
+分子 #7: T-complex protein 1 subunit zeta
+分子 #8: T-complex protein 1 subunit alpha
+分子 #9: Outer capsid protein sigma-3
+分子 #10: ZINC ION
+分子 #11: 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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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
緩衝液 | pH: 7.5 |
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凍結 | 凍結剤: ETHANE |
-電子顕微鏡法
顕微鏡 | FEI TALOS ARCTICA |
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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: 36.0 e/Å2 |
電子線 | 加速電圧: 200 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 |
実験機器 | モデル: Talos Arctica / 画像提供: FEI Company |
-画像解析
初期モデル | モデルのタイプ: NONE |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 6.2 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 26000 |
初期 角度割当 | タイプ: MAXIMUM LIKELIHOOD |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD |