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基本情報
登録情報 | データベース: EMDB / ID: EMD-4970 | |||||||||||||||
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タイトル | Structure of the core TFIIH-XPA-DNA complex | |||||||||||||||
![]() | Composite map produced from focused refined maps (deposited as additional EM maps). | |||||||||||||||
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![]() | Complex / Helicase / Translocase / DNA repair | |||||||||||||||
機能・相同性 | ![]() nucleotide-excision repair factor 1 complex / nucleotide-excision repair involved in interstrand cross-link repair / nucleotide-excision repair, DNA damage recognition / MMXD complex / core TFIIH complex portion of holo TFIIH complex / Cytosolic iron-sulfur cluster assembly / central nervous system myelin formation / positive regulation of mitotic recombination / hair cell differentiation / hair follicle maturation ...nucleotide-excision repair factor 1 complex / nucleotide-excision repair involved in interstrand cross-link repair / nucleotide-excision repair, DNA damage recognition / MMXD complex / core TFIIH complex portion of holo TFIIH complex / Cytosolic iron-sulfur cluster assembly / central nervous system myelin formation / positive regulation of mitotic recombination / hair cell differentiation / hair follicle maturation / nucleotide-excision repair factor 3 complex / nucleotide-excision repair, preincision complex assembly / CAK-ERCC2 complex / UV protection / embryonic cleavage / DNA 5'-3' helicase / G protein-coupled receptor internalization / regulation of cyclin-dependent protein serine/threonine kinase activity / transcription factor TFIIH core complex / transcription factor TFIIH holo complex / UV-damage excision repair / nuclear thyroid hormone receptor binding / RNA Polymerase I Transcription Termination / transcription preinitiation complex / regulation of mitotic cell cycle phase transition / DNA 3'-5' helicase / RNA polymerase II general transcription initiation factor activity / transcription factor TFIID complex / 3'-5' DNA helicase activity / erythrocyte maturation / spinal cord development / hematopoietic stem cell proliferation / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / bone mineralization / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / 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 / mRNA Capping / ATPase activator activity / DNA topological change / intrinsic apoptotic signaling pathway by p53 class mediator / RNA Polymerase I Transcription Initiation / protein localization to nucleus / hematopoietic stem cell differentiation / embryonic organ development / positive regulation of transcription initiation by RNA polymerase II / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / transcription elongation by RNA polymerase I / Formation of HIV elongation complex in the absence of HIV Tat / response to UV / RNA Polymerase II Transcription Elongation / transcription by RNA polymerase I / Formation of RNA Pol II elongation complex / hormone-mediated signaling pathway / transcription-coupled nucleotide-excision repair / RNA Polymerase II Pre-transcription Events / extracellular matrix organization / DNA helicase activity / insulin-like growth factor receptor signaling pathway / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / post-embryonic development / determination of adult lifespan / nucleotide-excision repair / chromosome segregation / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / RNA Polymerase I Promoter Escape / promoter-specific chromatin binding / 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 / base-excision repair / NoRC negatively regulates rRNA expression / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / response to toxic substance / spindle / multicellular organism growth / intrinsic apoptotic signaling pathway in response to DNA damage / sequence-specific double-stranded DNA binding / intracellular protein localization / 4 iron, 4 sulfur cluster binding / response to oxidative stress / double-stranded DNA binding / 5'-3' DNA helicase activity / protein-macromolecule adaptor activity / damaged DNA binding / in utero embryonic development / transcription by RNA polymerase II 類似検索 - 分子機能 | |||||||||||||||
生物種 | ![]() | |||||||||||||||
手法 | 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度: 3.5 Å | |||||||||||||||
![]() | Kokic G / Chernev A / Tegunov D / Dienemann C / Urlaub H / Cramer P | |||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structural basis of TFIIH activation for nucleotide excision repair. 著者: Goran Kokic / Aleksandar Chernev / Dimitry Tegunov / Christian Dienemann / Henning Urlaub / Patrick Cramer / ![]() 要旨: Nucleotide excision repair (NER) is the major DNA repair pathway that removes UV-induced and bulky DNA lesions. There is currently no structure of NER intermediates, which form around the large ...Nucleotide excision repair (NER) is the major DNA repair pathway that removes UV-induced and bulky DNA lesions. There is currently no structure of NER intermediates, which form around the large multisubunit transcription factor IIH (TFIIH). Here we report the cryo-EM structure of an NER intermediate containing TFIIH and the NER factor XPA. Compared to its transcription conformation, the TFIIH structure is rearranged such that its ATPase subunits XPB and XPD bind double- and single-stranded DNA, consistent with their translocase and helicase activities, respectively. XPA releases the inhibitory kinase module of TFIIH, displaces a 'plug' element from the DNA-binding pore in XPD, and together with the NER factor XPG stimulates XPD activity. Our results explain how TFIIH is switched from a transcription to a repair factor, and provide the basis for a mechanistic analysis of the NER pathway. | |||||||||||||||
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 | EMマップ: ![]() ![]() ![]() |
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ダウンロードとリンク
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マップデータ | ![]() | 33.9 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 43.2 KB 43.2 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() ![]() | 11.4 KB 11.4 KB | 表示 表示 | ![]() |
画像 | ![]() | 98.3 KB | ||
マスクデータ | ![]() | 125 MB | ![]() | |
Filedesc metadata | ![]() | 8.8 KB | ||
その他 | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() | 112.8 MB 112.8 MB 38.7 MB 98.8 MB 98.8 MB 7.2 MB 6.4 MB 6.4 MB 5.4 MB | ||
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-検証レポート
文書・要旨 | ![]() | 401.3 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 400.8 KB | 表示 | |
XML形式データ | ![]() | 6.3 KB | 表示 | |
CIF形式データ | ![]() | 7.2 KB | 表示 | |
アーカイブディレクトリ | ![]() ![]() | HTTPS FTP |
-関連構造データ
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リンク
EMDBのページ | ![]() ![]() |
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「今月の分子」の関連する項目 |
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マップ
ファイル | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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注釈 | Composite map produced from focused refined maps (deposited as additional EM maps). | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 1.05 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
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試料の構成要素
+全体 : Core TFIIH-XPA-DNA complex
+超分子 #1: Core TFIIH-XPA-DNA complex
+超分子 #2: TFIIH-XPA
+超分子 #3: DNA
+分子 #1: DNA1
+分子 #2: DNA2
+分子 #3: General transcription and DNA repair factor IIH helicase subunit XPB
+分子 #4: General transcription factor IIH subunit 5
+分子 #5: TFIIH basal transcription factor complex helicase XPD subunit
+分子 #6: General transcription factor IIH subunit 3
+分子 #7: General transcription factor IIH subunit 2
+分子 #8: General transcription factor IIH subunit 4
+分子 #9: DNA repair protein complementing XP-A cells
+分子 #10: IRON/SULFUR CLUSTER
+分子 #11: 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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![]() | 単粒子再構成法 |
試料の集合状態 | particle |
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試料調製
緩衝液 | pH: 7.5 |
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グリッド | モデル: Quantifoil R2/2 / 材質: GOLD / 前処理 - タイプ: GLOW DISCHARGE |
凍結 | 凍結剤: ETHANE / チャンバー内湿度: 100 % / チャンバー内温度: 277 K / 装置: FEI VITROBOT MARK IV 詳細: 4 ul of sample was applied to glow-discharged grids which were blotted for 5s and plunge-frozen in liquid ethane.. |
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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 SUMMIT (4k x 4k) 平均電子線量: 41.0 e/Å2 |
電子線 | 加速電圧: 300 kV / 電子線源: ![]() |
電子光学系 | 照射モード: FLOOD BEAM / 撮影モード: BRIGHT FIELD / Cs: 2.7 mm / 倍率(公称値): 130000 |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |
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画像解析
初期モデル | モデルのタイプ: OTHER / 詳細: Ab-initio model created in CryoSPARC. |
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最終 再構成 | 想定した対称性 - 点群: C1 (非対称) / 解像度のタイプ: BY AUTHOR / 解像度: 3.5 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 使用した粒子像数: 227776 |
初期 角度割当 | タイプ: RANDOM ASSIGNMENT |
最終 角度割当 | タイプ: PROJECTION MATCHING |