+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-40485 | |||||||||
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タイトル | CCT-G beta 5 complex closed state 8 | |||||||||
マップデータ | ||||||||||
試料 |
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キーワード | CCT / Gb5 / complex / open / CHAPERONE | |||||||||
機能・相同性 | 機能・相同性情報 GTPase activator complex / light adaption / dark adaptation / G-protein gamma-subunit binding / negative regulation of voltage-gated calcium channel activity / 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 ...GTPase activator complex / light adaption / dark adaptation / G-protein gamma-subunit binding / negative regulation of voltage-gated calcium channel activity / 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 / tubulin complex assembly / chaperonin-containing T-complex / BBSome-mediated cargo-targeting to cilium / 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 / RHOBTB1 GTPase cycle / intermediate filament cytoskeleton / WD40-repeat domain binding / G protein-coupled dopamine receptor signaling pathway / 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 / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / GTPase activator activity / positive regulation of GTPase activity / acrosomal vesicle / cell projection / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / response to virus / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / cilium / G-protein activation / mRNA 5'-UTR binding / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through CDC42 / G beta:gamma signalling through BTK / ADP signalling through P2Y purinoceptor 12 / Glucagon-type ligand receptors / Adrenaline,noradrenaline inhibits insulin secretion / Vasopressin regulates renal water homeostasis via Aquaporins / G alpha (z) signalling events / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / ADORA2B mediated anti-inflammatory cytokines production / ADP signalling through P2Y purinoceptor 1 / G beta:gamma signalling through PI3Kgamma / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / azurophil granule lumen / GPER1 signaling / Inactivation, recovery and regulation of the phototransduction cascade / G-protein beta-subunit binding / unfolded protein binding / heterotrimeric G-protein complex / G alpha (12/13) signalling events / melanosome / protein folding / signaling receptor complex adaptor activity / Thrombin signalling through proteinase activated receptors (PARs) / presynapse / protein-folding chaperone binding / Ca2+ pathway / cell body / G alpha (i) signalling events / G alpha (s) signalling events / G alpha (q) signalling events / secretory granule lumen / ficolin-1-rich granule lumen / microtubule / Extra-nuclear estrogen signaling / cytoskeleton / protein stabilization / cadherin binding / G protein-coupled receptor signaling pathway / GTPase activity / centrosome / ubiquitin protein ligase binding / Neutrophil degranulation / Golgi apparatus / signal transduction / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding / nucleus 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: 2.8 Å | |||||||||
データ登録者 | Wang S / Sass M / Willardson BM / Shen PS | |||||||||
資金援助 | 米国, 1件
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引用 | ジャーナル: Mol Cell / 年: 2023 タイトル: Visualizing the chaperone-mediated folding trajectory of the G protein β5 β-propeller. 著者: Shuxin Wang / Mikaila I Sass / Yujin Kwon / W Grant Ludlam / Theresa M Smith / Ethan J Carter / Nathan E Gladden / Margot Riggi / Janet H Iwasa / Barry M Willardson / Peter S Shen / 要旨: The Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with β-propeller domains. Here, ...The Chaperonin Containing Tailless polypeptide 1 (CCT) complex is an essential protein folding machine with a diverse clientele of substrates, including many proteins with β-propeller domains. Here, we determine the structures of human CCT in complex with its accessory co-chaperone, phosducin-like protein 1 (PhLP1), in the process of folding Gβ, a component of Regulator of G protein Signaling (RGS) complexes. Cryoelectron microscopy (cryo-EM) and image processing reveal an ensemble of distinct snapshots that represent the folding trajectory of Gβ from an unfolded molten globule to a fully folded β-propeller. These structures reveal the mechanism by which CCT directs Gβ folding through initiating specific intermolecular contacts that facilitate the sequential folding of individual β sheets until the propeller closes into its native structure. This work directly visualizes chaperone-mediated protein folding and establishes that CCT orchestrates folding by stabilizing intermediates through interactions with surface residues that permit the hydrophobic core to coalesce into its folded state. | |||||||||
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_40485.map.gz | 50.2 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-40485-v30.xml emd-40485.xml | 29 KB 29 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_40485_fsc.xml | 9.9 KB | 表示 | FSCデータファイル |
画像 | emd_40485.png | 532.7 KB | ||
Filedesc metadata | emd-40485.cif.gz | 9 KB | ||
その他 | emd_40485_half_map_1.map.gz emd_40485_half_map_2.map.gz | 73.1 MB 73.1 MB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-40485 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-40485 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_40485_validation.pdf.gz | 1.1 MB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_40485_full_validation.pdf.gz | 1.1 MB | 表示 | |
XML形式データ | emd_40485_validation.xml.gz | 18.5 KB | 表示 | |
CIF形式データ | emd_40485_validation.cif.gz | 23.8 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-40485 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-40485 | HTTPS FTP |
-関連構造データ
関連構造データ | 8sheMC 8sfeC 8sffC 8sg8C 8sg9C 8sgcC 8sglC 8sgqC 8sh9C 8shaC 8shdC 8shfC 8shgC 8shlC 8shnC 8shoC 8shpC 8shqC 8shtC 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 (文献) |
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類似構造データ | 類似検索 - 機能・相同性F&H 検索 |
-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_40485.map.gz / 形式: CCP4 / 大きさ: 103 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: 1.058 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
-ハーフマップ: #2
ファイル | emd_40485_half_map_1.map | ||||||||||||
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投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: #1
ファイル | emd_40485_half_map_2.map | ||||||||||||
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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 : CCT-Gb5-PhLP1 in closed state 8
+超分子 #1: CCT-Gb5-PhLP1 in closed state 8
+分子 #1: Guanine nucleotide-binding protein subunit beta-5
+分子 #2: T-complex protein 1 subunit alpha
+分子 #3: T-complex protein 1 subunit beta
+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 gamma
+分子 #7: T-complex protein 1 subunit eta, N-terminally processed
+分子 #8: T-complex protein 1 subunit theta
+分子 #9: T-complex protein 1 subunit zeta
+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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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-試料調製
濃度 | 1.5 mg/mL | |||||||||||||||||||||
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緩衝液 | pH: 7.5 構成要素:
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凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 277.15 K / 装置: FEI VITROBOT MARK I | |||||||||||||||||||||
詳細 | The sample was monodisperse |
-電子顕微鏡法
顕微鏡 | TFS KRIOS |
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撮影 | フィルム・検出器のモデル: GATAN K3 (6k x 4k) / 平均電子線量: 40.42 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): 1.2 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 |