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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-8664 | |||||||||
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| タイトル | Nucleotide-driven Triple-state Remodeling of the AAA-ATPase Channel in the Activated Human 26S Proteasome | |||||||||
マップデータ | Activated Human 26S Proteasome | |||||||||
試料 |
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キーワード | 26S proteasome / ATP-dependent protease / AAA-ATPase / peptide-unfolding channel / 20S core particle / HYDROLASE | |||||||||
| 機能・相同性 | 機能・相同性情報thyrotropin-releasing hormone receptor binding / nuclear proteasome complex / host-mediated perturbation of viral transcription / 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 / purine ribonucleoside triphosphate binding / meiosis I / proteasome regulatory particle / cytosolic proteasome complex ...thyrotropin-releasing hormone receptor binding / nuclear proteasome complex / host-mediated perturbation of viral transcription / 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 / 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 / protein K63-linked deubiquitination / negative regulation of programmed cell death / Regulation of ornithine decarboxylase (ODC) / Proteasome assembly / Cross-presentation of soluble exogenous antigens (endosomes) / proteasome core complex / Somitogenesis / K63-linked deubiquitinase activity / proteasome binding / transcription factor binding / regulation of protein catabolic process / myofibril / proteasome storage granule / general transcription initiation factor binding / blastocyst development / positive regulation of RNA polymerase II transcription preinitiation complex assembly / polyubiquitin modification-dependent protein binding / immune system process / protein deubiquitination / 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 / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / enzyme regulator activity / regulation of proteasomal protein catabolic process / ERAD pathway / inclusion body / TBP-class protein binding / proteolysis involved in protein catabolic process / proteasome complex / sarcomere / Regulation of activated PAK-2p34 by proteasome mediated degradation / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / stem cell differentiation / 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 / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / negative regulation of inflammatory response to antigenic stimulus / Degradation of AXIN / lipopolysaccharide binding / P-body / Hh mutants are degraded by ERAD / Activation of NF-kappaB in B cells / Degradation of GLI1 by the proteasome / G2/M Checkpoints / Hedgehog ligand biogenesis / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Defective CFTR causes cystic fibrosis / Autodegradation of the E3 ubiquitin ligase COP1 / Negative regulation of NOTCH4 signaling / Regulation of RUNX3 expression and activity / Vif-mediated degradation of APOBEC3G / Hedgehog 'on' state / 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 / double-strand break repair via homologous recombination / Degradation of beta-catenin by the destruction complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / ABC-family proteins mediated transport / double-strand break repair via nonhomologous end joining / CDK-mediated phosphorylation and removal of Cdc6 / CLEC7A (Dectin-1) signaling / SCF(Skp2)-mediated degradation of p27/p21 / response to virus / FCERI mediated NF-kB activation / Regulation of expression of SLITs and ROBOs / Metalloprotease DUBs 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: 4.2 Å | |||||||||
データ登録者 | Zhu Y / Wang WL | |||||||||
引用 | ジャーナル: Nat Commun / 年: 2018タイトル: Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome. 著者: Yanan Zhu / Wei Li Wang / Daqi Yu / Qi Ouyang / Ying Lu / Youdong Mao / ![]() 要旨: The proteasome is a sophisticated ATP-dependent molecular machine responsible for protein degradation in all known eukaryotic cells. It remains elusive how conformational changes of the AAA-ATPase ...The proteasome is a sophisticated ATP-dependent molecular machine responsible for protein degradation in all known eukaryotic cells. It remains elusive how conformational changes of the AAA-ATPase unfoldase in the regulatory particle (RP) control the gating of the substrate-translocation channel leading to the proteolytic chamber of the core particle (CP). Here we report three alternative states of the ATP-γ-S-bound human proteasome, in which the CP gates are asymmetrically open, visualized by cryo-EM at near-atomic resolutions. At least four nucleotides are bound to the AAA-ATPase ring in these open-gate states. Variation in nucleotide binding gives rise to an axial movement of the pore loops narrowing the substrate-translation channel, which exhibit remarkable structural transitions between the spiral-staircase and saddle-shaped-circle topologies. Gate opening in the CP is thus regulated by nucleotide-driven conformational changes of the AAA-ATPase unfoldase. These findings demonstrate an elegant mechanism of allosteric coordination among sub-machines within the human proteasome holoenzyme. | |||||||||
| 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: SurfView Molmil Jmol/JSmol |
| 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_8664.map.gz | 612.8 MB | EMDBマップデータ形式 | |
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| ヘッダ (付随情報) | emd-8664-v30.xml emd-8664.xml | 57.9 KB 57.9 KB | 表示 表示 | EMDBヘッダ |
| 画像 | emd_8664.png | 174.3 KB | ||
| Filedesc metadata | emd-8664.cif.gz | 13.4 KB | ||
| その他 | emd_8664_additional_1.map.gz emd_8664_additional_2.map.gz | 591 MB 613.7 MB | ||
| アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-8664 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-8664 | HTTPS FTP |
-検証レポート
| 文書・要旨 | emd_8664_validation.pdf.gz | 706.3 KB | 表示 | EMDB検証レポート |
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| 文書・詳細版 | emd_8664_full_validation.pdf.gz | 705.8 KB | 表示 | |
| XML形式データ | emd_8664_validation.xml.gz | 6.8 KB | 表示 | |
| CIF形式データ | emd_8664_validation.cif.gz | 8.1 KB | 表示 | |
| アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8664 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8664 | HTTPS FTP |
-関連構造データ
| 関連構造データ | ![]() 5vfqMC ![]() 8662C ![]() 8663C ![]() 8665C ![]() 8666C ![]() 8667C ![]() 8668C ![]() 5vfoC ![]() 5vfpC ![]() 5vfrC ![]() 5vfsC ![]() 5vftC ![]() 5vfuC 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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| 類似構造データ | |
| 電子顕微鏡画像生データ | EMPIAR-10090 (タイトル: Nucleotide-Driven Triple-State Remodeling of the AAA-ATPase Channel in the Activated Human 26S ProteasomeData size: 2.8 TB Data #1: Motion-corrected single frame micrographs of ATP-gS-bound human proteasome [micrographs - single frame] Data #2: Single-particle stacks of classified conformations [picked particles - multiframe - processed]) |
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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 |
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マップ
| ファイル | ダウンロード / ファイル: emd_8664.map.gz / 形式: CCP4 / 大きさ: 669.9 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| 注釈 | Activated Human 26S Proteasome | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| 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: 0.75 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: Activated Human 26S Proteasome, additional map #1
| ファイル | emd_8664_additional_1.map | ||||||||||||
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| 注釈 | Activated Human 26S Proteasome, additional map #1 | ||||||||||||
| 投影像・断面図 |
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| 密度ヒストグラム |
-追加マップ: Activated Human 26S Proteasome, additional map #2
| ファイル | emd_8664_additional_2.map | ||||||||||||
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| 注釈 | Activated Human 26S Proteasome, additional 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 : 26S proteasome bound to ATP-gammaS
+超分子 #1: 26S proteasome bound to ATP-gammaS
+分子 #1: Proteasome subunit alpha type-6
+分子 #2: Proteasome subunit alpha type-2
+分子 #3: Proteasome subunit alpha type-4
+分子 #4: Proteasome subunit alpha type-7
+分子 #5: Proteasome subunit alpha type-5
+分子 #6: Proteasome subunit alpha type-1
+分子 #7: Proteasome subunit alpha type-3
+分子 #8: Proteasome subunit beta type-6
+分子 #9: Proteasome subunit beta type-7
+分子 #10: Proteasome subunit beta type-3
+分子 #11: Proteasome subunit beta type-2
+分子 #12: Proteasome subunit beta type-5
+分子 #13: Proteasome subunit beta type-1
+分子 #14: Proteasome subunit beta type-4
+分子 #15: 26S proteasome non-ATPase regulatory subunit 1
+分子 #16: 26S proteasome non-ATPase regulatory subunit 3
+分子 #17: 26S proteasome non-ATPase regulatory subunit 12
+分子 #18: 26S proteasome non-ATPase regulatory subunit 11
+分子 #19: 26S proteasome non-ATPase regulatory subunit 6
+分子 #20: 26S proteasome non-ATPase regulatory subunit 7
+分子 #21: 26S proteasome non-ATPase regulatory subunit 13
+分子 #22: 26S proteasome non-ATPase regulatory subunit 4
+分子 #23: 26S proteasome non-ATPase regulatory subunit 14
+分子 #24: 26S proteasome non-ATPase regulatory subunit 8
+分子 #25: Sem1
+分子 #26: 26S proteasome regulatory subunit 7
+分子 #27: 26S proteasome regulatory subunit 4
+分子 #28: 26S proteasome regulatory subunit 8
+分子 #29: 26S proteasome regulatory subunit 6B
+分子 #30: 26S proteasome regulatory subunit 10B
+分子 #31: 26S proteasome regulatory subunit 6A
+分子 #32: 26S proteasome non-ATPase regulatory subunit 2
+分子 #33: ZINC ION
+分子 #34: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
-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 |
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試料調製
| 緩衝液 | pH: 7.5 |
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| 凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
| 顕微鏡 | FEI TECNAI 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: 30.0 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 |
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画像解析
| 初期モデル | モデルのタイプ: OTHER |
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| 最終 再構成 | 想定した対称性 - 点群: C1 (非対称) / 解像度のタイプ: BY AUTHOR / 解像度: 4.2 Å / 解像度の算出法: FSC 0.143 CUT-OFF / ソフトウェア - 名称: RELION (ver. 1.3) / 使用した粒子像数: 66246 |
| 初期 角度割当 | タイプ: ANGULAR RECONSTITUTION / ソフトウェア - 名称: RELION (ver. 1.3) |
| 最終 角度割当 | タイプ: PROJECTION MATCHING / ソフトウェア - 名称: RELION (ver. 1.3) |
-原子モデル構築 1
| 精密化 | 空間: REAL / 温度因子: 70 |
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| 得られたモデル | ![]() PDB-5vfq: |
ムービー
コントローラー
万見について



キーワード
Homo sapiens (ヒト)
データ登録者
引用

UCSF Chimera
































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Y (Row.)
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