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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-4089 | |||||||||
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| タイトル | The human 26S Proteasome at 6.8 Ang. | |||||||||
マップデータ | ||||||||||
試料 |
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キーワード | 26S Proteasome / Cryo-EM / Single Particle Analysis / Homology Modelling / 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 / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / 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 / positive regulation of inclusion body assembly / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / 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 / 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 / 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) / Somitogenesis / Resolution of D-loop Structures through Holliday Junction Intermediates / 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 / 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 / mRNA export from nucleus / 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 / P-body / Hh mutants are degraded by ERAD / lipopolysaccharide binding / 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 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: 6.8 Å | |||||||||
データ登録者 | Schweitzer A / Beck F | |||||||||
引用 | ジャーナル: Mol Cell Proteomics / 年: 2017タイトル: Molecular Details Underlying Dynamic Structures and Regulation of the Human 26S Proteasome. 著者: Xiaorong Wang / Peter Cimermancic / Clinton Yu / Andreas Schweitzer / Nikita Chopra / James L Engel / Charles Greenberg / Alexander S Huszagh / Florian Beck / Eri Sakata / Yingying Yang / ...著者: Xiaorong Wang / Peter Cimermancic / Clinton Yu / Andreas Schweitzer / Nikita Chopra / James L Engel / Charles Greenberg / Alexander S Huszagh / Florian Beck / Eri Sakata / Yingying Yang / Eric J Novitsky / Alexander Leitner / Paolo Nanni / Abdullah Kahraman / Xing Guo / Jack E Dixon / Scott D Rychnovsky / Ruedi Aebersold / Wolfgang Baumeister / Andrej Sali / Lan Huang / ![]() 要旨: The 26S proteasome is the macromolecular machine responsible for ATP/ubiquitin dependent degradation. As aberration in proteasomal degradation has been implicated in many human diseases, structural ...The 26S proteasome is the macromolecular machine responsible for ATP/ubiquitin dependent degradation. As aberration in proteasomal degradation has been implicated in many human diseases, structural analysis of the human 26S proteasome complex is essential to advance our understanding of its action and regulation mechanisms. In recent years, cross-linking mass spectrometry (XL-MS) has emerged as a powerful tool for elucidating structural topologies of large protein assemblies, with its unique capability of studying protein complexes in cells. To facilitate the identification of cross-linked peptides, we have previously developed a robust amine reactive sulfoxide-containing MS-cleavable cross-linker, disuccinimidyl sulfoxide (DSSO). To better understand the structure and regulation of the human 26S proteasome, we have established new DSSO-based and XL-MS workflows by coupling with HB-tag based affinity purification to comprehensively examine protein-protein interactions within the 26S proteasome. In total, we have identified 447 unique lysine-to-lysine linkages delineating 67 interprotein and 26 intraprotein interactions, representing the largest cross-link dataset for proteasome complexes. In combination with EM maps and computational modeling, the architecture of the 26S proteasome was determined to infer its structural dynamics. In particular, three proteasome subunits Rpn1, Rpn6, and Rpt6 displayed multiple conformations that have not been previously reported. Additionally, cross-links between proteasome subunits and 15 proteasome interacting proteins including 9 known and 6 novel ones have been determined to demonstrate their physical interactions at the amino acid level. Our results have provided new insights on the dynamics of the 26S human proteasome and the methodologies presented here can be applied to study other protein complexes. | |||||||||
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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 |
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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_4089.map.gz | 5.3 MB | EMDBマップデータ形式 | |
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| ヘッダ (付随情報) | emd-4089-v30.xml emd-4089.xml | 48.9 KB 48.9 KB | 表示 表示 | EMDBヘッダ |
| 画像 | emd_4089.png | 191.3 KB | ||
| Filedesc metadata | emd-4089.cif.gz | 13.3 KB | ||
| アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-4089 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4089 | HTTPS FTP |
-検証レポート
| 文書・要旨 | emd_4089_validation.pdf.gz | 216.9 KB | 表示 | EMDB検証レポート |
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| 文書・詳細版 | emd_4089_full_validation.pdf.gz | 216.1 KB | 表示 | |
| XML形式データ | emd_4089_validation.xml.gz | 6.2 KB | 表示 | |
| アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4089 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4089 | HTTPS FTP |
-関連構造データ
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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_4089.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: 2.16 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 proteasome non-ATPase regulatory subunit 2
+分子 #2: Proteasome subunit beta type-6
+分子 #3: Proteasome subunit beta type-7
+分子 #4: Proteasome subunit beta type-3
+分子 #5: Proteasome subunit beta type-2
+分子 #6: Proteasome subunit beta type-5
+分子 #7: Proteasome subunit beta type-1
+分子 #8: Proteasome subunit beta type-4
+分子 #9: Proteasome subunit alpha type-6
+分子 #10: Proteasome subunit alpha type-2
+分子 #11: Proteasome subunit alpha type-4
+分子 #12: Proteasome subunit alpha type-7
+分子 #13: Proteasome subunit alpha type-5
+分子 #14: Proteasome subunit alpha type-1
+分子 #15: Proteasome subunit alpha type-3
+分子 #16: 26S protease regulatory subunit 7
+分子 #17: 26S protease regulatory subunit 4
+分子 #18: 26S protease regulatory subunit 8
+分子 #19: 26S protease regulatory subunit 6B
+分子 #20: 26S protease regulatory subunit 10B
+分子 #21: 26S protease regulatory subunit 6A
+分子 #22: 26S proteasome non-ATPase regulatory subunit 1
+分子 #23: 26S proteasome non-ATPase regulatory subunit 13
+分子 #24: 26S proteasome non-ATPase regulatory subunit 12
+分子 #25: 26S proteasome non-ATPase regulatory subunit 11
+分子 #26: 26S proteasome non-ATPase regulatory subunit 6
+分子 #27: 26S proteasome non-ATPase regulatory subunit 3
+分子 #28: 26S proteasome non-ATPase regulatory subunit 8
+分子 #29: 26S proteasome non-ATPase regulatory subunit 7
+分子 #30: 26S proteasome non-ATPase regulatory subunit 14
+分子 #31: 26S proteasome non-ATPase regulatory subunit 4
+分子 #32: 26S proteasome complex subunit DSS1
-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
| 濃度 | 0.5 mg/mL |
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| 緩衝液 | pH: 7.5 |
| 糖包埋 | 材質: ice |
| 凍結 | 凍結剤: ETHANE |
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電子顕微鏡法
| 顕微鏡 | FEI TITAN KRIOS |
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| 撮影 | フィルム・検出器のモデル: FEI FALCON II (4k x 4k) 検出モード: INTEGRATING / 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: 1-7 / 撮影したグリッド数: 8 / 実像数: 31857 / 平均電子線量: 45.0 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 / 最大 デフォーカス(公称値): 3.5 µm / 最小 デフォーカス(公称値): 0.8 µm |
| 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 |
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画像解析
| 初期モデル | モデルのタイプ: EMDB MAP EMDB ID: |
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| 最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 6.8 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 252000 |
| 初期 角度割当 | タイプ: PROJECTION MATCHING |
| 最終 角度割当 | タイプ: PROJECTION MATCHING |
-原子モデル構築 1
| 精密化 | 空間: REAL / プロトコル: FLEXIBLE FIT |
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| 得られたモデル | ![]() PDB-5ln3: |
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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

















Z (Sec.)
Y (Row.)
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