+データを開く
-基本情報
登録情報 | データベース: EMDB / ID: EMD-14209 | |||||||||
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タイトル | Proteasome-ZFAND5 Complex Z-A state | |||||||||
マップデータ | ZFAND5-proteasome complex Z-A state | |||||||||
試料 |
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機能・相同性 | 機能・相同性情報 Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / modulation by host of viral transcription / 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 / positive regulation of proteasomal protein catabolic process / proteasome regulatory particle ...Impaired BRCA2 translocation to the nucleus / Impaired BRCA2 binding to SEM1 (DSS1) / modulation by host of viral transcription / 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 / positive regulation of proteasomal protein catabolic process / proteasome regulatory particle / cytosolic proteasome complex / proteasome regulatory particle, lid subcomplex / proteasome-activating activity / proteasome regulatory particle, base subcomplex / protein K63-linked deubiquitination / metal-dependent deubiquitinase activity / regulation of endopeptidase activity / 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 / Homologous DNA Pairing and Strand Exchange / Regulation of ornithine decarboxylase (ODC) / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / proteasome core complex / Resolution of D-loop Structures through Holliday Junction Intermediates / Cross-presentation of soluble exogenous antigens (endosomes) / Somitogenesis / K63-linked deubiquitinase activity / Impaired BRCA2 binding to RAD51 / immune system process / myofibril / proteasome binding / regulation of protein catabolic process / proteasome storage granule / Presynaptic phase of homologous DNA pairing and strand exchange / blastocyst development / NF-kappaB binding / endopeptidase activator activity / polyubiquitin modification-dependent protein binding / proteasome assembly / proteasome endopeptidase complex / proteasome core complex, beta-subunit complex / proteasome core complex, alpha-subunit complex / threonine-type endopeptidase activity / mRNA export from nucleus / enzyme regulator activity / regulation of proteasomal protein catabolic process / inclusion body / negative regulation of inflammatory response to antigenic stimulus / : / sarcomere / proteasome complex / Regulation of activated PAK-2p34 by proteasome mediated degradation / ciliary basal body / proteolysis involved in protein catabolic process / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / 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 / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Degradation of DVL / stem cell differentiation / CDK-mediated phosphorylation and removal of Cdc6 / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Hh mutants are degraded by ERAD / lipopolysaccharide binding / SCF(Skp2)-mediated degradation of p27/p21 / Degradation of AXIN / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Hedgehog ligand biogenesis / Defective CFTR causes cystic fibrosis / Negative regulation of NOTCH4 signaling / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / G2/M Checkpoints / Vif-mediated degradation of APOBEC3G / Autodegradation of the E3 ubiquitin ligase COP1 / Hedgehog 'on' state / Regulation of RUNX3 expression and activity / P-body / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / Orc1 removal from chromatin / double-strand break repair via homologous recombination / 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 / response to virus / Degradation of beta-catenin by the destruction complex / protein catabolic process / ABC-family proteins mediated transport / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha 類似検索 - 分子機能 | |||||||||
生物種 | Homo sapiens (ヒト) / human (ヒト) | |||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 4.7 Å | |||||||||
データ登録者 | Zhu Y / Lu Y | |||||||||
資金援助 | 1件
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引用 | ジャーナル: To Be Published タイトル: Mechanism of 26S proteasome activation by the 19S-interacting protein ZFAND5 著者: Zhu Y / Lu Y | |||||||||
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_14209.map.gz | 113.7 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-14209-v30.xml emd-14209.xml | 43.3 KB 43.3 KB | 表示 表示 | EMDBヘッダ |
画像 | emd_14209.png | 76.6 KB | ||
アーカイブディレクトリ | http://ftp.pdbj.org/pub/emdb/structures/EMD-14209 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-14209 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_14209_validation.pdf.gz | 612.8 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_14209_full_validation.pdf.gz | 612.4 KB | 表示 | |
XML形式データ | emd_14209_validation.xml.gz | 6.5 KB | 表示 | |
CIF形式データ | emd_14209_validation.cif.gz | 7.5 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-14209 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-14209 | HTTPS FTP |
-関連構造データ
関連構造データ | 7qy7MC 7qxnC 7qxpC 7qxuC 7qxwC 7qxxC 7qyaC 7qybC 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_14209.map.gz / 形式: CCP4 / 大きさ: 125 MB / タイプ: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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注釈 | ZFAND5-proteasome complex Z-A state | ||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.37 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
-試料の構成要素
+全体 : human proteasome zfand5 complex Z-A state
+超分子 #1: human proteasome zfand5 complex Z-A state
+分子 #1: 26S proteasome non-ATPase regulatory subunit 13
+分子 #2: 26S proteasome non-ATPase regulatory subunit 4
+分子 #3: 26S proteasome non-ATPase regulatory subunit 14
+分子 #4: 26S proteasome non-ATPase regulatory subunit 8
+分子 #5: 26S proteasome complex subunit SEM1
+分子 #6: 26S proteasome non-ATPase regulatory subunit 2
+分子 #7: 26S proteasome non-ATPase regulatory subunit 1
+分子 #8: 26S proteasome non-ATPase regulatory subunit 3
+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 7
+分子 #13: 26S protease regulatory subunit 7
+分子 #14: 26S protease regulatory subunit 4
+分子 #15: PSMC5 isoform 15
+分子 #16: 26S protease regulatory subunit 6B
+分子 #17: 26S proteasome regulatory subunit 10B
+分子 #18: 26S protease regulatory subunit 6A
+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: Isoform Long of 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: ZINC ION
+分子 #34: ADENOSINE-5'-TRIPHOSPHATE
-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 | 2 mg/mL |
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緩衝液 | pH: 7 |
凍結 | 凍結剤: ETHANE |
-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: GATAN K2 QUANTUM (4k x 4k) 平均電子線量: 46.6 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): 2.5 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 |
-画像解析
最終 再構成 | 解像度のタイプ: BY AUTHOR / 解像度: 4.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 34363 |
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初期 角度割当 | タイプ: MAXIMUM LIKELIHOOD |
最終 角度割当 | タイプ: MAXIMUM LIKELIHOOD |