+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 5fur | ||||||
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タイトル | Structure of human TFIID-IIA bound to core promoter DNA | ||||||
要素 |
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キーワード | TRANSCRIPTION / TFIID / TFIIA / RNA POLYMERASE II / GENERAL TRANSCRIPTION FACTORS / PREINITIATION COMPLEX / CORE PROMOTER / DNA BINDING | ||||||
機能・相同性 | 機能・相同性情報 spermine transport / negative regulation of MHC class I biosynthetic process / DNA-templated transcription open complex formation / TFIIH-class transcription factor complex binding / negative regulation of protein autoubiquitination / transcription factor TFTC complex / negative regulation of MHC class II biosynthetic process / RNA polymerase transcription factor SL1 complex / regulation of cell cycle G1/S phase transition / RNA polymerase I general transcription initiation factor activity ...spermine transport / negative regulation of MHC class I biosynthetic process / DNA-templated transcription open complex formation / TFIIH-class transcription factor complex binding / negative regulation of protein autoubiquitination / transcription factor TFTC complex / negative regulation of MHC class II biosynthetic process / RNA polymerase transcription factor SL1 complex / regulation of cell cycle G1/S phase transition / RNA polymerase I general transcription initiation factor activity / SLIK (SAGA-like) complex / RNA polymerase III general transcription initiation factor activity / RNA polymerase I core promoter sequence-specific DNA binding / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Polymerase III Transcription Initiation From Type 3 Promoter / RNA Polymerase III Abortive And Retractive Initiation / positive regulation of androgen receptor activity / maintenance of protein location in nucleus / transcription factor TFIIA complex / female germ cell nucleus / male pronucleus / female pronucleus / transcription regulator inhibitor activity / RNA polymerase II general transcription initiation factor binding / nuclear vitamin D receptor binding / regulation of fat cell differentiation / RNA Polymerase I Transcription Termination / transcription preinitiation complex / SAGA complex / nuclear thyroid hormone receptor binding / inner cell mass cell proliferation / midbrain development / cellular response to ATP / histone acetyltransferase binding / transcription factor TFIID complex / RNA polymerase II general transcription initiation factor activity / HIV Transcription Initiation / RNA Polymerase II HIV Promoter Escape / Transcription of the HIV genome / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA Polymerase I Transcription Initiation / ubiquitin conjugating enzyme activity / aryl hydrocarbon receptor binding / transcription initiation at RNA polymerase I promoter / MLL1 complex / TFIIB-class transcription factor binding / transcription by RNA polymerase III / RNA polymerase II transcribes snRNA genes / negative regulation of cell cycle / P-TEFb complex binding / positive regulation of transcription initiation by RNA polymerase II / RNA polymerase II core promoter sequence-specific DNA binding / negative regulation of ubiquitin-dependent protein catabolic process / positive regulation of intrinsic apoptotic signaling pathway / regulation of DNA repair / core promoter sequence-specific DNA binding / histone acetyltransferase activity / RNA polymerase II preinitiation complex assembly / histone acetyltransferase / RNA Polymerase II Pre-transcription Events / estrogen receptor signaling pathway / TBP-class protein binding / SIRT1 negatively regulates rRNA expression / regulation of signal transduction by p53 class mediator / male germ cell nucleus / DNA-templated transcription initiation / nuclear receptor binding / peptidyl-threonine phosphorylation / transcription initiation at RNA polymerase II promoter / RNA Polymerase I Promoter Escape / lysine-acetylated histone binding / negative regulation of protein kinase activity / mRNA transcription by RNA polymerase II / NoRC negatively regulates rRNA expression / euchromatin / B-WICH complex positively regulates rRNA expression / response to organic cyclic compound / protein polyubiquitination / cellular response to UV / G2/M transition of mitotic cell cycle / p53 binding / positive regulation of protein binding / cell junction / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / kinase activity / peptidyl-serine phosphorylation / ubiquitin-dependent protein catabolic process / spermatogenesis / DNA-binding transcription factor binding / RNA polymerase II-specific DNA-binding transcription factor binding / Estrogen-dependent gene expression / Regulation of TP53 Activity through Phosphorylation / transcription regulator complex / sequence-specific DNA binding / protein autophosphorylation / transcription by RNA polymerase II 類似検索 - 分子機能 | ||||||
生物種 | HOMO SAPIENS (ヒト) | ||||||
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: 8.5 Å | ||||||
データ登録者 | Louder, R.K. / He, Y. / Lopez-Blanco, J.R. / Fang, J. / Chacon, P. / Nogales, E. | ||||||
引用 | ジャーナル: Nature / 年: 2016 タイトル: Structure of promoter-bound TFIID and model of human pre-initiation complex assembly. 著者: Robert K Louder / Yuan He / José Ramón López-Blanco / Jie Fang / Pablo Chacón / Eva Nogales / 要旨: The general transcription factor IID (TFIID) plays a central role in the initiation of RNA polymerase II (Pol II)-dependent transcription by nucleating pre-initiation complex (PIC) assembly at the ...The general transcription factor IID (TFIID) plays a central role in the initiation of RNA polymerase II (Pol II)-dependent transcription by nucleating pre-initiation complex (PIC) assembly at the core promoter. TFIID comprises the TATA-binding protein (TBP) and 13 TBP-associated factors (TAF1-13), which specifically interact with a variety of core promoter DNA sequences. Here we present the structure of human TFIID in complex with TFIIA and core promoter DNA, determined by single-particle cryo-electron microscopy at sub-nanometre resolution. All core promoter elements are contacted by subunits of TFIID, with TAF1 and TAF2 mediating major interactions with the downstream promoter. TFIIA bridges the TBP-TATA complex with lobe B of TFIID. We also present the cryo-electron microscopy reconstruction of a fully assembled human TAF-less PIC. Superposition of common elements between the two structures provides novel insights into the general role of TFIID in promoter recognition, PIC assembly, and transcription initiation. | ||||||
履歴 |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN **-STRANDED BARREL THIS IS REPRESENTED BY A **-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-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: MolmilJmol/JSmol |
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 5fur.cif.gz | 545.9 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb5fur.ent.gz | 397 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 5fur.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
文書・要旨 | 5fur_validation.pdf.gz | 789 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 5fur_full_validation.pdf.gz | 994.8 KB | 表示 | |
XML形式データ | 5fur_validation.xml.gz | 98.4 KB | 表示 | |
CIF形式データ | 5fur_validation.cif.gz | 145.9 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/fu/5fur ftp://data.pdbj.org/pub/pdb/validation_reports/fu/5fur | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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1 |
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-要素
-タンパク質 , 1種, 1分子 A
#1: タンパク質 | 分子量: 37729.938 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) HOMO SAPIENS (ヒト) / 参照: UniProt: P20226 |
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-TRANSCRIPTION INITIATION FACTOR IIA SUBUNIT ... , 3種, 3分子 BCD
#2: タンパク質・ペプチド | 分子量: 5098.864 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) HOMO SAPIENS (ヒト) / 細胞株: HELA / 参照: UniProt: P52655 |
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#3: タンパク質・ペプチド | 分子量: 5594.344 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) HOMO SAPIENS (ヒト) / 細胞株: HELA / 参照: UniProt: P52655 |
#4: タンパク質 | 分子量: 11275.824 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) HOMO SAPIENS (ヒト) / 細胞株: HELA / 参照: UniProt: P52657 |
-DNA鎖 , 2種, 2分子 EF
#5: DNA鎖 | 分子量: 27664.635 Da / 分子数: 1 / Fragment: NONTEMPLATE STRAND / 由来タイプ: 天然 詳細: A COMPOSITE SEQUENCE COMBINING SEVERAL PROMOTER MOTIFS FROM HUMANS A 由来: (天然) HOMO SAPIENS (ヒト) / 細胞株: HELA |
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#6: DNA鎖 | 分子量: 28485.129 Da / 分子数: 1 / Fragment: TEMPLATE STRAND / 由来タイプ: 天然 詳細: A COMPOSITE SEQUENCE COMBINING SEVERAL PROMOTER MOTIFS FROM HUMANS A 由来: (天然) HOMO SAPIENS (ヒト) / 細胞株: HELA |
-TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT ... , 5種, 6分子 GHIJKL
#7: タンパク質 | 分子量: 215152.406 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) HOMO SAPIENS (ヒト) / 細胞株: HELA 参照: UniProt: P21675, histone acetyltransferase, non-specific serine/threonine protein kinase | ||
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#8: タンパク質 | 分子量: 40325.117 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) HOMO SAPIENS (ヒト) / 細胞株: HELA / 参照: UniProt: Q15545 | ||
#9: タンパク質 | 分子量: 137159.984 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) HOMO SAPIENS (ヒト) / 細胞株: HELA / 参照: UniProt: Q6P1X5 | ||
#10: タンパク質 | 分子量: 72749.297 Da / 分子数: 2 / 由来タイプ: 天然 / 由来: (天然) HOMO SAPIENS (ヒト) / 細胞株: HELA / 参照: UniProt: P49848 #11: タンパク質 | | 分子量: 34304.359 Da / 分子数: 1 / 由来タイプ: 天然 / 由来: (天然) HOMO SAPIENS (ヒト) / 細胞株: HELA / 参照: UniProt: Q7Z7C8 |
-詳細
配列の詳細 | THE SUPER CORE PROMOTER SEQUENCE IS DESCRIBED IN JUVEN- GERSHON. ET AL. (2006) NATURE METHODS, 3, P.917-922. |
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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 |
-試料調製
構成要素 | 名称: HUMAN TFIID-TFIIA COMPLEX BOUND TO SUPER CORE PROMOTER DNA タイプ: COMPLEX |
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緩衝液 | 名称: 10 MM HEPES, 10 MM MGCL2, 50 MM KCL, 3% TREHALOSE 1 MM DTT, 0.0125% NP-40 pH: 7.9 詳細: 10 MM HEPES, 10 MM MGCL2, 50 MM KCL, 3% TREHALOSE 1 MM DTT, 0.0125% NP-40 |
試料 | 濃度: 0.05 mg/ml / 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
試料支持 | 詳細: CARBON |
急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 詳細: LIQUID ETHANE |
-電子顕微鏡撮影
顕微鏡 | モデル: FEI TITAN / 日付: 2014年8月11日 詳細: THE CAMERA WAS OPERATED IN COUNTING MODE WITH A DOSE RATE OF 8 ELECTRONS PER PIXEL PER SECOND, WITH A TOTAL EXPOSURE TIME OF 10 SECONDS FRACTIONATED OVER 20 FRAMES. |
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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 / 倍率(補正後): 37879 X / 最大 デフォーカス(公称値): 4000 nm / 最小 デフォーカス(公称値): 2000 nm / Cs: 2.7 mm |
撮影 | 電子線照射量: 46 e/Å2 フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
画像スキャン | デジタル画像の数: 1253 |
-解析
EMソフトウェア |
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CTF補正 | 詳細: EACH PARTICLE | ||||||||||||||||||||
対称性 | 点対称性: C1 (非対称) | ||||||||||||||||||||
3次元再構成 | 解像度: 8.5 Å / 粒子像の数: 22050 / ピクセルサイズ(実測値): 1.32 Å 詳細: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD-3305. (DEPOSITION ID: 14001). 対称性のタイプ: POINT | ||||||||||||||||||||
原子モデル構築 | 空間: REAL | ||||||||||||||||||||
精密化 | 最高解像度: 8.5 Å | ||||||||||||||||||||
精密化ステップ | サイクル: LAST / 最高解像度: 8.5 Å
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