+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-8674 | |||||||||
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タイトル | Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle | |||||||||
マップデータ | Final map of human proteasome RP in the T1 state corrected with a B-factor of -80 | |||||||||
試料 |
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キーワード | p28 / 26S proteasome / regulatory particle / 19S / gankyrin / HYDROLASE | |||||||||
機能・相同性 | 機能・相同性情報 cytoplasmic sequestering of NF-kappaB / positive regulation of inclusion body assembly / proteasome regulatory particle assembly / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / thyrotropin-releasing hormone receptor binding / modulation by host of viral transcription / meiosis I / 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 ...cytoplasmic sequestering of NF-kappaB / positive regulation of inclusion body assembly / proteasome regulatory particle assembly / Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / thyrotropin-releasing hormone receptor binding / modulation by host of viral transcription / meiosis I / 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 / proteasome regulatory particle / cytosolic proteasome complex / positive regulation of proteasomal protein catabolic process / proteasome regulatory particle, lid subcomplex / proteasome-activating activity / proteasome regulatory particle, base subcomplex / metal-dependent deubiquitinase activity / negative regulation of programmed cell death / protein K63-linked deubiquitination / 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) / Regulation of ornithine decarboxylase (ODC) / Resolution of D-loop Structures through Holliday Junction Intermediates / intermediate filament cytoskeleton / Cross-presentation of soluble exogenous antigens (endosomes) / K63-linked deubiquitinase activity / Somitogenesis / Impaired BRCA2 binding to RAD51 / negative regulation of NF-kappaB transcription factor activity / proteasome binding / negative regulation of release of cytochrome c from mitochondria / transcription factor binding / regulation of protein catabolic process / proteasome storage granule / Presynaptic phase of homologous DNA pairing and strand exchange / negative regulation of DNA damage response, signal transduction by p53 class mediator / blastocyst development / positive regulation of cyclin-dependent protein serine/threonine kinase activity / general transcription initiation factor binding / endopeptidase activator activity / polyubiquitin modification-dependent protein binding / proteasome assembly / protein deubiquitination / positive regulation of RNA polymerase II transcription preinitiation complex assembly / negative regulation of MAPK cascade / mRNA export from nucleus / regulation of proteasomal protein catabolic process / enzyme regulator activity / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / inclusion body / ERAD pathway / cytoskeletal protein binding / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / positive regulation of protein ubiquitination / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / protein localization to plasma membrane / Asymmetric localization of PCP proteins / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / TNFR2 non-canonical NF-kB pathway / stem cell differentiation / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling / Hh mutants are degraded by ERAD / Degradation of AXIN / Activation of NF-kappaB in B cells / Degradation of GLI1 by the proteasome / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / G2/M Checkpoints / Negative regulation of NOTCH4 signaling / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Autodegradation of the E3 ubiquitin ligase COP1 / Vif-mediated degradation of APOBEC3G / double-strand break repair via homologous recombination / P-body / Regulation of RUNX3 expression and activity / 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 / MAPK6/MAPK4 signaling / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / Degradation of beta-catenin by the destruction complex / ABC-family proteins mediated transport / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / HDR through Homologous Recombination (HRR) 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: 5.7 Å | |||||||||
データ登録者 | Lu Y / Wu J | |||||||||
引用 | ジャーナル: Mol Cell / 年: 2017 タイトル: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle. 著者: Ying Lu / Jiayi Wu / Yuanchen Dong / Shuobing Chen / Shuangwu Sun / Yong-Bei Ma / Qi Ouyang / Daniel Finley / Marc W Kirschner / Youdong Mao / 要旨: The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of ...The proteasome holoenzyme is activated by its regulatory particle (RP) consisting of two subcomplexes, the lid and the base. A key event in base assembly is the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembly chaperones in mammals: PAAF1, p28/gankyrin, p27/PSMD9, and S5b. Using cryogenic electron microscopy, we analyzed the non-AAA structure of the p28-bound human RP at 4.5 Å resolution and determined seven distinct conformations of the Rpn1-p28-AAA subcomplex within the p28-bound RP at subnanometer resolutions. Remarkably, the p28-bound AAA ring does not form a channel in the free RP and spontaneously samples multiple "open" and "closed" topologies at the Rpt2-Rpt6 and Rpt3-Rpt4 interfaces. Our analysis suggests that p28 assists the proteolytic core particle to select a specific conformation of the ATPase ring for RP engagement and is released in a shoehorn-like fashion in the last step of the chaperone-mediated proteasome assembly. | |||||||||
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_8674.map.gz | 58.1 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-8674-v30.xml emd-8674.xml | 36.9 KB 36.9 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_8674.png | 77.3 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-8674 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-8674 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_8674_validation.pdf.gz | 562.7 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_8674_full_validation.pdf.gz | 562.3 KB | 表示 | |
XML形式データ | emd_8674_validation.xml.gz | 6 KB | 表示 | |
CIF形式データ | emd_8674_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-8674 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-8674 | HTTPS FTP |
-関連構造データ
関連構造データ | 5vhfMC 8672C 8675C 8676C 8677C 8678C 8679C 8680C 8681C 8682C 8683C 8684C 5vgzC 5vhhC 5vhiC 5vhjC 5vhmC 5vhnC 5vhoC 5vhpC 5vhqC 5vhrC 5vhsC C: 同じ文献を引用 (文献) 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-10091 (タイトル: Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle Data size: 70.0 Data #1: Classified single-particle datasets for multiple conformations of p28-bound human regulatory complex [picked particles - multiframe - processed]) |
-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_8674.map.gz / 形式: CCP4 / 大きさ: 64 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Final map of human proteasome RP in the T1 state corrected with a B-factor of -80 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 0.98 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 : Proteasome regulatory particle
+超分子 #1: Proteasome regulatory particle
+分子 #1: 26S proteasome non-ATPase regulatory subunit 10
+分子 #2: 26S proteasome regulatory subunit 7
+分子 #3: 26S proteasome regulatory subunit 4
+分子 #4: 26S proteasome regulatory subunit 8
+分子 #5: 26S proteasome regulatory subunit 6B
+分子 #6: 26S proteasome regulatory subunit 10B
+分子 #7: 26S proteasome regulatory subunit 6A
+分子 #8: 26S proteasome non-ATPase regulatory subunit 1
+分子 #9: 26S proteasome non-ATPase regulatory subunit 3
+分子 #10: 26S proteasome non-ATPase regulatory subunit 12
+分子 #11: 26S proteasome non-ATPase regulatory subunit 11
+分子 #12: 26S proteasome non-ATPase regulatory subunit 6
+分子 #13: 26S proteasome non-ATPase regulatory subunit 7
+分子 #14: 26S proteasome non-ATPase regulatory subunit 13
+分子 #15: 26S proteasome non-ATPase regulatory subunit 4
+分子 #16: 26S proteasome non-ATPase regulatory subunit 14
+分子 #17: 26S proteasome non-ATPase regulatory subunit 8
+分子 #18: 26S proteasome complex subunit SEM1
+分子 #19: 26S proteasome non-ATPase regulatory subunit 2
+分子 #20: ZINC ION
-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 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: 50.0 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: INSILICO MODEL |
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最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 5.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 39520 |
初期 角度割当 | タイプ: ANGULAR RECONSTITUTION |
最終 角度割当 | タイプ: PROJECTION MATCHING |