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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: PDB / ID: 6t9l | |||||||||
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| タイトル | SAGA DUB module bound to a ubiqitinated nucleosome | |||||||||
要素 |
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キーワード | GENE REGULATION / Coactivator / Transcription / Histone acetyltransferase / Histone deubiquitinase | |||||||||
| 機能・相同性 | 機能・相同性情報DUBm complex / RITS complex assembly / regulation of nucleocytoplasmic transport / transcription export complex 2 / regulatory ncRNA-mediated heterochromatin formation / nuclear mRNA surveillance / post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery / SLIK (SAGA-like) complex / regulation of protein localization to chromatin / SAGA complex ...DUBm complex / RITS complex assembly / regulation of nucleocytoplasmic transport / transcription export complex 2 / regulatory ncRNA-mediated heterochromatin formation / nuclear mRNA surveillance / post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery / SLIK (SAGA-like) complex / regulation of protein localization to chromatin / SAGA complex / poly(A)+ mRNA export from nucleus / positive regulation of RNA polymerase II transcription preinitiation complex assembly / protein deubiquitination / Ub-specific processing proteases / nuclear pore / mRNA export from nucleus / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / IRAK2 mediated activation of TAK1 complex / Prevention of phagosomal-lysosomal fusion / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Endosomal Sorting Complex Required For Transport (ESCRT) / Membrane binding and targetting of GAG proteins / Negative regulation of FLT3 / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Constitutive Signaling by NOTCH1 HD Domain Mutants / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / APC-Cdc20 mediated degradation of Nek2A / p75NTR recruits signalling complexes / RNA splicing / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / Regulation of pyruvate metabolism / NF-kB is activated and signals survival / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Pexophagy / Regulation of innate immune responses to cytosolic DNA / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation / Activated NOTCH1 Transmits Signal to the Nucleus / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / Regulation of BACH1 activity / Translesion synthesis by POLK / InlB-mediated entry of Listeria monocytogenes into host cell / MAP3K8 (TPL2)-dependent MAPK1/3 activation / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / Translesion synthesis by POLI / IKK complex recruitment mediated by RIP1 / Gap-filling DNA repair synthesis and ligation in GG-NER / PINK1-PRKN Mediated Mitophagy / Regulation of activated PAK-2p34 by proteasome mediated degradation / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / TCF dependent signaling in response to WNT / Autodegradation of Cdh1 by Cdh1:APC/C / Regulation of NF-kappa B signaling / APC/C:Cdc20 mediated degradation of Securin / activated TAK1 mediates p38 MAPK activation / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / Regulation of signaling by CBL / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / TNFR2 non-canonical NF-kB pathway / NOTCH3 Activation and Transmission of Signal to the Nucleus / AUF1 (hnRNP D0) binds and destabilizes mRNA / Negative regulators of DDX58/IFIH1 signaling / Fanconi Anemia Pathway / Peroxisomal protein import / Deactivation of the beta-catenin transactivating complex / P-body / Negative regulation of FGFR3 signaling / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Stabilization of p53 / transcription elongation by RNA polymerase II / Negative regulation of FGFR2 signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A 類似検索 - 分子機能 | |||||||||
| 生物種 | ![]() Homo sapiens (ヒト)synthetic construct (人工物) | |||||||||
| 手法 | 電子顕微鏡法 / 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.6 Å | |||||||||
データ登録者 | Wang, H. / Cramer, P. | |||||||||
| 資金援助 | ドイツ, 2件
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引用 | ジャーナル: Nature / 年: 2020タイトル: Structure of the transcription coactivator SAGA. 著者: Haibo Wang / Christian Dienemann / Alexandra Stützer / Henning Urlaub / Alan C M Cheung / Patrick Cramer / ![]() 要旨: Gene transcription by RNA polymerase II is regulated by activator proteins that recruit the coactivator complexes SAGA (Spt-Ada-Gcn5-acetyltransferase) and transcription factor IID (TFIID). SAGA is ...Gene transcription by RNA polymerase II is regulated by activator proteins that recruit the coactivator complexes SAGA (Spt-Ada-Gcn5-acetyltransferase) and transcription factor IID (TFIID). SAGA is required for all regulated transcription and is conserved among eukaryotes. SAGA contains four modules: the activator-binding Tra1 module, the core module, the histone acetyltransferase (HAT) module and the histone deubiquitination (DUB) module. Previous studies provided partial structures, but the structure of the central core module is unknown. Here we present the cryo-electron microscopy structure of SAGA from the yeast Saccharomyces cerevisiae and resolve the core module at 3.3 Å resolution. The core module consists of subunits Taf5, Sgf73 and Spt20, and a histone octamer-like fold. The octamer-like fold comprises the heterodimers Taf6-Taf9, Taf10-Spt7 and Taf12-Ada1, and two histone-fold domains in Spt3. Spt3 and the adjacent subunit Spt8 interact with the TATA box-binding protein (TBP). The octamer-like fold and its TBP-interacting region are similar in TFIID, whereas Taf5 and the Taf6 HEAT domain adopt distinct conformations. Taf12 and Spt20 form flexible connections to the Tra1 module, whereas Sgf73 tethers the DUB module. Binding of a nucleosome to SAGA displaces the HAT and DUB modules from the core-module surface, allowing the DUB module to bind one face of an ubiquitinated nucleosome. | |||||||||
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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 | 分子: Molmil Jmol/JSmol |
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ダウンロードとリンク
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ダウンロード
| PDBx/mmCIF形式 | 6t9l.cif.gz | 432 KB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb6t9l.ent.gz | 322 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 6t9l.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
| その他 | その他のダウンロード |
-検証レポート
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/t9/6t9l ftp://data.pdbj.org/pub/pdb/validation_reports/t9/6t9l | HTTPS FTP |
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-関連構造データ
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リンク
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集合体
| 登録構造単位 | ![]()
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要素
-タンパク質 , 8種, 11分子 AEBFCGDHKLO
| #1: タンパク質 | 分子量: 15303.930 Da / 分子数: 2 / 由来タイプ: 組換発現 由来: (組換発現) 発現宿主: ![]() #2: タンパク質 | 分子量: 11263.231 Da / 分子数: 2 / 由来タイプ: 組換発現 由来: (組換発現) 発現宿主: ![]() #3: タンパク質 | 分子量: 13978.241 Da / 分子数: 2 / 由来タイプ: 組換発現 由来: (組換発現) 遺伝子: hist1h2aj, LOC494591 / 発現宿主: ![]() #4: タンパク質 | | 分子量: 13524.752 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) 発現宿主: ![]() #5: タンパク質 | | 分子量: 13848.097 Da / 分子数: 1 / 由来タイプ: 組換発現 由来: (組換発現) 発現宿主: ![]() #8: タンパク質 | | 分子量: 53692.270 Da / 分子数: 1 / 由来タイプ: 組換発現 / 詳細: This is a zinc containing protein. 由来: (組換発現) ![]() 遺伝子: UBP8, YMR223W, YM9959.05 / 発現宿主: ![]() #9: タンパク質 | | 分子量: 11094.497 Da / 分子数: 1 / 由来タイプ: 天然 由来: (天然) ![]() 参照: UniProt: Q6WNK7 #12: タンパク質 | | 分子量: 8576.831 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: UBC / 発現宿主: ![]() |
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-Widom601 DNA (145- ... , 2種, 2分子 IJ
| #6: DNA鎖 | 分子量: 44520.383 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) synthetic construct (人工物) |
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| #7: DNA鎖 | 分子量: 44991.660 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) synthetic construct (人工物) |
-SAGA-associated factor ... , 2種, 2分子 MN
| #10: タンパク質 | 分子量: 11297.625 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: This a zinc-finger containing protein. 由来: (天然) ![]() 参照: UniProt: Q03067 |
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| #11: タンパク質 | 分子量: 72976.688 Da / 分子数: 1 / 由来タイプ: 天然 / 詳細: This a zinc-finger containing protein. 由来: (天然) ![]() 参照: UniProt: P53165 |
-非ポリマー , 1種, 8分子 
| #13: 化合物 | ChemComp-ZN / |
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-詳細
| 研究の焦点であるリガンドがあるか | N |
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-実験情報
-実験
| 実験 | 手法: 電子顕微鏡法 |
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| EM実験 | 試料の集合状態: PARTICLE / 3次元再構成法: 単粒子再構成法 |
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試料調製
| 構成要素 |
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| 分子量 | 値: 0.25 MDa / 実験値: NO | ||||||||||||||||||||||||||||||||||||||||||
| 由来(天然) |
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| 由来(組換発現) |
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| 緩衝液 | pH: 7.5 / 詳細: Solution were made from stock solution | ||||||||||||||||||||||||||||||||||||||||||
| 緩衝液成分 |
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| 試料 | 濃度: 0.2 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | ||||||||||||||||||||||||||||||||||||||||||
| 急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 100 % / 凍結前の試料温度: 277 K / 詳細: blot for 4 seconds before plunging |
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電子顕微鏡撮影
| 実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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| 顕微鏡 | モデル: FEI TITAN KRIOS |
| 電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
| 電子レンズ | モード: BRIGHT FIELD / Cs: 2.7 mm / C2レンズ絞り径: 70 µm / アライメント法: COMA FREE |
| 試料ホルダ | 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER |
| 撮影 | 平均露光時間: 9 sec. / 電子線照射量: 44.17 e/Å2 / 検出モード: COUNTING フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
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解析
| EMソフトウェア |
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| CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||
| 粒子像の選択 | 選択した粒子像数: 313986 | ||||||||||||||||||||||||||||
| 対称性 | 点対称性: C1 (非対称) | ||||||||||||||||||||||||||||
| 3次元再構成 | 解像度: 3.6 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 113856 / クラス平均像の数: 1 / 対称性のタイプ: POINT | ||||||||||||||||||||||||||||
| 原子モデル構築 | B value: 114.6 / プロトコル: RIGID BODY FIT / 空間: REAL / Target criteria: Correlation coefficient | ||||||||||||||||||||||||||||
| 原子モデル構築 | PDB-ID: 4ZUX Accession code: 4ZUX / Source name: PDB / タイプ: experimental model |
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万見について





Homo sapiens (ヒト)
ドイツ, 2件
引用
UCSF Chimera















PDBj
























































