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基本情報
登録情報 | データベース: PDB / ID: 7nvw | ||||||||||||||||||
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タイトル | TFIIH in a pre-translocated state (without ADP-BeF3) | ||||||||||||||||||
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![]() | TRANSCRIPTION / Initiation | ||||||||||||||||||
機能・相同性 | ![]() core TFIIH complex portion of holo TFIIH complex / MMXD complex / Cytosolic iron-sulfur cluster assembly / nucleotide-excision repair, DNA duplex unwinding / central nervous system myelin formation / positive regulation of mitotic recombination / hair follicle maturation / hair cell differentiation / ventricular system development / nucleotide-excision repair factor 3 complex ...core TFIIH complex portion of holo TFIIH complex / MMXD complex / Cytosolic iron-sulfur cluster assembly / nucleotide-excision repair, DNA duplex unwinding / central nervous system myelin formation / positive regulation of mitotic recombination / hair follicle maturation / hair cell differentiation / ventricular system development / nucleotide-excision repair factor 3 complex / cyclin-dependent protein kinase activating kinase holoenzyme complex / transcription factor TFIIE complex / nucleotide-excision repair, preincision complex assembly / UV protection / CAK-ERCC2 complex / transcription factor TFIIK complex / embryonic cleavage / transcription open complex formation at RNA polymerase II promoter / adult heart development / G protein-coupled receptor internalization / DNA 3'-5' helicase / transcription factor TFIIH core complex / cyclin-dependent protein serine/threonine kinase activator activity / transcription factor TFIIH holo complex / transcription preinitiation complex / RNA Polymerase I Transcription Termination / nuclear thyroid hormone receptor binding / regulation of mitotic cell cycle phase transition / hematopoietic stem cell proliferation / regulation of cyclin-dependent protein serine/threonine kinase activity / spinal cord development / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / mRNA Capping / bone mineralization / 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 / erythrocyte maturation / regulation of G1/S transition of mitotic cell cycle / 3'-5' DNA helicase activity / RNA Polymerase I Transcription Initiation / transcription by RNA polymerase I / DNA topological change / ATPase activator activity / RNA polymerase II transcribes snRNA genes / transcription factor TFIID complex / intrinsic apoptotic signaling pathway by p53 class mediator / RNA polymerase II general transcription initiation factor activity / hematopoietic stem cell differentiation / transcription elongation by RNA polymerase I / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / embryonic organ development / transcription-coupled nucleotide-excision repair / Formation of HIV elongation complex in the absence of HIV Tat / Cyclin E associated events during G1/S transition / RNA Polymerase II Transcription Elongation / Cyclin A/B1/B2 associated events during G2/M transition / Formation of RNA Pol II elongation complex / response to UV / Cyclin A:Cdk2-associated events at S phase entry / DNA helicase activity / RNA Polymerase II Pre-transcription Events / hormone-mediated signaling pathway / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / extracellular matrix organization / insulin-like growth factor receptor signaling pathway / post-embryonic development / chromosome segregation / transcription elongation by RNA polymerase II / determination of adult lifespan / promoter-specific chromatin binding / nucleotide-excision repair / RNA Polymerase I Promoter Escape / transcription initiation at RNA polymerase II promoter / TP53 Regulates Transcription of DNA Repair Genes / positive regulation of smooth muscle cell proliferation / NoRC negatively regulates rRNA expression / protein localization / multicellular organism growth / Dual Incision in GG-NER / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / cellular response to gamma radiation / Formation of Incision Complex in GG-NER / response to calcium ion / spindle / Dual incision in TC-NER / G1/S transition of mitotic cell cycle / Gap-filling DNA repair synthesis and ligation in TC-NER / Cyclin D associated events in G1 / protein-macromolecule adaptor activity / RUNX1 regulates transcription of genes involved in differentiation of HSCs 類似検索 - 分子機能 | ||||||||||||||||||
生物種 | ![]() ![]() | ||||||||||||||||||
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: 4.3 Å | ||||||||||||||||||
![]() | Aibara, S. / Schilbach, S. / Cramer, P. | ||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structures of mammalian RNA polymerase II pre-initiation complexes. 著者: Shintaro Aibara / Sandra Schilbach / Patrick Cramer / ![]() 要旨: The initiation of transcription is a focal point for the regulation of gene activity during mammalian cell differentiation and development. To initiate transcription, RNA polymerase II (Pol II) ...The initiation of transcription is a focal point for the regulation of gene activity during mammalian cell differentiation and development. To initiate transcription, RNA polymerase II (Pol II) assembles with general transcription factors into a pre-initiation complex (PIC) that opens promoter DNA. Previous work provided the molecular architecture of the yeast and human PIC and a topological model for DNA opening by the general transcription factor TFIIH. Here we report the high-resolution cryo-electron microscopy structure of PIC comprising human general factors and Sus scrofa domesticus Pol II, which is 99.9% identical to human Pol II. We determine the structures of PIC with closed and opened promoter DNA at 2.5-2.8 Å resolution, and resolve the structure of TFIIH at 2.9-4.0 Å resolution. We capture the TFIIH translocase XPB in the pre- and post-translocation states, and show that XPB induces and propagates a DNA twist to initiate the opening of DNA approximately 30 base pairs downstream of the TATA box. We also provide evidence that DNA opening occurs in two steps and leads to the detachment of TFIIH from the core PIC, which may stop DNA twisting and enable RNA chain initiation. | ||||||||||||||||||
履歴 |
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構造の表示
ムービー |
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構造ビューア | 分子: ![]() ![]() |
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PDBx/mmCIF形式 | ![]() | 555.7 KB | 表示 | ![]() |
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PDB形式 | ![]() | 441.7 KB | 表示 | ![]() |
PDBx/mmJSON形式 | ![]() | ツリー表示 | ![]() | |
その他 | ![]() |
-検証レポート
文書・要旨 | ![]() | 704.6 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 728.7 KB | 表示 | |
XML形式データ | ![]() | 84.6 KB | 表示 | |
CIF形式データ | ![]() | 120.3 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
関連構造データ | ![]() 12615MC ![]() 7nvrC ![]() 7nvsC ![]() 7nvtC ![]() 7nvuC ![]() 7nvvC ![]() 7nvxC ![]() 7nvyC ![]() 7nvzC ![]() 7nw0C M: このデータのモデリングに利用したマップデータ C: 同じ文献を引用 ( |
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類似構造データ |
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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 , 2種, 2分子 03
#1: タンパク質 | 分子量: 87021.078 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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#4: タンパク質 | 分子量: 35873.965 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
-General transcription ... , 7種, 7分子 124567W
#2: タンパク質 | 分子量: 62116.492 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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#3: タンパク質 | 分子量: 52245.156 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
#5: タンパク質 | 分子量: 34416.008 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
#6: タンパク質 | 分子量: 8060.362 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
#7: タンパク質 | 分子量: 44481.996 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
#8: タンパク質 | 分子量: 89404.734 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
#11: タンパク質 | 分子量: 49516.094 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() |
-DNA鎖 , 2種, 2分子 NT
#9: DNA鎖 | 分子量: 32911.859 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) ![]() |
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#10: DNA鎖 | 分子量: 32508.752 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) ![]() |
-Unassigned Peptide, likely ... , 2種, 2分子 YZ
#12: タンパク質・ペプチド | 分子量: 698.854 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
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#13: タンパク質・ペプチド | 分子量: 1635.006 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() |
-非ポリマー , 2種, 8分子 ![](data/chem/img/SF4.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/ZN.gif)
#14: 化合物 | ChemComp-SF4 / |
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#15: 化合物 | ChemComp-ZN / |
-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 | 名称: TFIIH (without ADP-BeF3) / タイプ: COMPLEX / Entity ID: #1-#13 / 由来: MULTIPLE SOURCES |
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分子量 | 値: 0.49 MDa / 実験値: NO |
緩衝液 | pH: 7.5 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
急速凍結 | 凍結剤: ETHANE |
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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: ![]() |
電子レンズ | モード: BRIGHT FIELD |
撮影 | 電子線照射量: 41.1 e/Å2 フィルム・検出器のモデル: GATAN K3 BIOQUANTUM (6k x 4k) |
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解析
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3次元再構成 | 解像度: 4.3 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 129156 / 対称性のタイプ: POINT |