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基本情報
登録情報 | データベース: EMDB / ID: EMD-9512 | ||||||||||||
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タイトル | Cryo-EM map of the human 26S proteasome at 3.5A resolution with C2 symmetry | ||||||||||||
![]() | with C2 symmetry | ||||||||||||
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![]() | protein complex / human proteasome / HYDROLASE | ||||||||||||
機能・相同性 | ![]() thyrotropin-releasing hormone receptor binding / nuclear proteasome complex / host-mediated perturbation of viral transcription / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / positive regulation of inclusion body assembly / 加水分解酵素; プロテアーゼ; ペプチド結合加水分解酵素; オメガペプチターゼ / proteasome accessory complex / integrator complex / purine ribonucleoside triphosphate binding ...thyrotropin-releasing hormone receptor binding / nuclear proteasome complex / host-mediated perturbation of viral transcription / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / positive regulation of inclusion body assembly / 加水分解酵素; プロテアーゼ; ペプチド結合加水分解酵素; オメガペプチターゼ / proteasome accessory complex / integrator complex / purine ribonucleoside triphosphate binding / meiosis I / proteasome regulatory particle / cytosolic proteasome complex / positive regulation of proteasomal protein catabolic process / proteasome-activating activity / proteasome regulatory particle, lid subcomplex / proteasome regulatory particle, base subcomplex / metal-dependent deubiquitinase activity / negative regulation of programmed cell death / protein K63-linked deubiquitination / Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / proteasome core complex / Resolution of D-loop Structures through Holliday Junction Intermediates / Somitogenesis / K63-linked deubiquitinase activity / Impaired BRCA2 binding to RAD51 / proteasome binding / transcription factor binding / regulation of protein catabolic process / myofibril / proteasome storage granule / Presynaptic phase of homologous DNA pairing and strand exchange / general transcription initiation factor binding / blastocyst development / polyubiquitin modification-dependent protein binding / protein deubiquitination / positive regulation of RNA polymerase II transcription preinitiation complex assembly / regulation of proteasomal protein catabolic process / NF-kappaB binding / proteasome endopeptidase complex / endopeptidase activator activity / proteasome core complex, beta-subunit complex / proteasome assembly / threonine-type endopeptidase activity / proteasome core complex, alpha-subunit complex / mRNA export from nucleus / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / enzyme regulator activity / immune system process / inclusion body / ERAD pathway / Regulation of activated PAK-2p34 by proteasome mediated degradation / Autodegradation of Cdh1 by Cdh1:APC/C / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / NIK-->noncanonical NF-kB signaling / SCF-beta-TrCP mediated degradation of Emi1 / proteasome complex / proteolysis involved in protein catabolic process / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / TBP-class protein binding / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Degradation of DVL / Dectin-1 mediated noncanonical NF-kB signaling / sarcomere / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Degradation of AXIN / Hh mutants are degraded by ERAD / Activation of NF-kappaB in B cells / Degradation of GLI1 by the proteasome / Hedgehog ligand biogenesis / G2/M Checkpoints / Defective CFTR causes cystic fibrosis / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Autodegradation of the E3 ubiquitin ligase COP1 / Negative regulation of NOTCH4 signaling / Vif-mediated degradation of APOBEC3G / Regulation of RUNX3 expression and activity / Hedgehog 'on' state / double-strand break repair via homologous recombination / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / MAPK6/MAPK4 signaling / stem cell differentiation / Degradation of beta-catenin by the destruction complex / lipopolysaccharide binding 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: 3.5 Å | ||||||||||||
![]() | Huang XL / Luan B / Wu JP / Shi YG | ||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: An atomic structure of the human 26S proteasome. 著者: Xiuliang Huang / Bai Luan / Jianping Wu / Yigong Shi / ![]() 要旨: We report the cryo-EM structure of the human 26S proteasome at an average resolution of 3.5 Å, allowing atomic modeling of 28 subunits in the core particle (CP) and 18 subunits in the regulatory ...We report the cryo-EM structure of the human 26S proteasome at an average resolution of 3.5 Å, allowing atomic modeling of 28 subunits in the core particle (CP) and 18 subunits in the regulatory particle (RP). The C-terminal residues of Rpt3 and Rpt5 subunits in the RP can be seen inserted into surface pockets formed between adjacent α subunits in the CP. Each of the six Rpt subunits contains a bound nucleotide, and the central gate of the CP α-ring is closed despite RP association. The six pore 1 loops in the Rpt ring are arranged similarly to a spiral staircase along the axial channel of substrate transport, which is constricted by the pore 2 loops. We also determined the cryo-EM structure of the human proteasome bound to the deubiquitinating enzyme USP14 at 4.35-Å resolution. Together, our structures provide a framework for mechanistic understanding of eukaryotic proteasome function. | ||||||||||||
履歴 |
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構造の表示
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構造ビューア | EMマップ: ![]() ![]() ![]() |
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マップデータ | ![]() | 478.8 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 53.1 KB 53.1 KB | 表示 表示 | ![]() |
画像 | ![]() | 32.5 KB | ||
Filedesc metadata | ![]() | 13.9 KB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 611.6 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 611.2 KB | 表示 | |
XML形式データ | ![]() | 7.8 KB | 表示 | |
CIF形式データ | ![]() | 9.1 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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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 | with C2 symmetry | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.07 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
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試料の構成要素
+全体 : human 26S proteasome
+超分子 #1: human 26S proteasome
+分子 #1: 26S protease regulatory subunit 4
+分子 #2: 26S protease regulatory subunit 7
+分子 #3: 26S protease regulatory subunit 10B
+分子 #4: 26S protease regulatory subunit 6A
+分子 #5: 26S protease regulatory subunit 8
+分子 #6: 26S protease regulatory subunit 6B
+分子 #7: 26S proteasome non-ATPase regulatory subunit 1
+分子 #8: 26S proteasome non-ATPase regulatory subunit 13
+分子 #9: 26S proteasome non-ATPase regulatory subunit 12
+分子 #10: 26S proteasome non-ATPase regulatory subunit 11
+分子 #11: 26S proteasome non-ATPase regulatory subunit 6
+分子 #12: 26S proteasome non-ATPase regulatory subunit 3
+分子 #13: 26S proteasome non-ATPase regulatory subunit 8
+分子 #14: 26S proteasome non-ATPase regulatory subunit 7
+分子 #15: 26S proteasome non-ATPase regulatory subunit 14
+分子 #16: 26S proteasome non-ATPase regulatory subunit 4
+分子 #17: 26S proteasome complex subunit DSS1
+分子 #18: 26S proteasome non-ATPase regulatory subunit 2
+分子 #19: Proteasome subunit alpha type-6
+分子 #20: Proteasome subunit alpha type-2
+分子 #21: Proteasome subunit alpha type-4
+分子 #22: Proteasome subunit alpha type-7
+分子 #23: Proteasome subunit alpha type-5
+分子 #24: Proteasome subunit alpha type-1
+分子 #25: Proteasome subunit alpha type-3
+分子 #26: Proteasome subunit beta type-6
+分子 #27: Proteasome subunit beta type-7
+分子 #28: Proteasome subunit beta type-3
+分子 #29: Proteasome subunit beta type-2
+分子 #30: Proteasome subunit beta type-5
+分子 #31: Proteasome subunit beta type-1
+分子 #32: Proteasome subunit beta type-4
+分子 #33: 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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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
濃度 | 1 mg/mL | ||||||||||||
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緩衝液 | pH: 8 構成要素:
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グリッド | 材質: COPPER / 支持フィルム - 材質: CARBON / 支持フィルム - トポロジー: CONTINUOUS / 支持フィルム - Film thickness: 3 / 前処理 - タイプ: GLOW DISCHARGE / 前処理 - 時間: 30 sec. / 前処理 - 雰囲気: AIR | ||||||||||||
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 281 K / 装置: FEI VITROBOT MARK IV / 詳細: blot for 2 seconds before plunging. | ||||||||||||
詳細 | This sample was monodisperse. |
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電子顕微鏡法
顕微鏡 | FEI TITAN KRIOS |
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温度 | 最低: 70.0 K |
詳細 | Preliminary grid screening was performed manually |
撮影 | フィルム・検出器のモデル: FEI FALCON II (4k x 4k) デジタル化 - サイズ - 横: 4096 pixel / デジタル化 - サイズ - 縦: 4096 pixel / デジタル化 - 画像ごとのフレーム数: 1-26 / 平均露光時間: 1.6 sec. / 平均電子線量: 37.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 最大 デフォーカス(補正後): 0.0026000000000000003 µm 最小 デフォーカス(補正後): 0.0016 µm / 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm |
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 |