+データを開く
-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 | |||||||||||||||
マップデータ | Composite map produced from focused refined maps (deposited as additional EM maps). | |||||||||||||||
試料 |
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キーワード | Complex / Helicase / Translocase / DNA repair | |||||||||||||||
機能・相同性 | 機能・相同性情報 nucleotide-excision repair factor 1 complex / nucleotide-excision repair involved in interstrand cross-link repair / nucleotide-excision repair, DNA damage recognition / 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 / response to auditory stimulus / positive regulation of mitotic recombination ...nucleotide-excision repair factor 1 complex / nucleotide-excision repair involved in interstrand cross-link repair / nucleotide-excision repair, DNA damage recognition / 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 / response to auditory stimulus / positive regulation of mitotic recombination / hair follicle maturation / hair cell differentiation / nucleotide-excision repair factor 3 complex / nucleotide-excision repair, preincision complex assembly / CAK-ERCC2 complex / UV protection / embryonic cleavage / G protein-coupled receptor internalization / UV-damage excision repair / DNA 3'-5' helicase / transcription factor TFIIH core complex / 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 / intercellular bridge / 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 / 3'-5' DNA helicase activity / RNA Polymerase I Transcription Initiation / transcription by RNA polymerase I / DNA topological change / ATPase activator activity / transcription factor TFIID complex / intrinsic apoptotic signaling pathway by p53 class mediator / protein localization to nucleus / 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 / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / response to UV / DNA helicase activity / RNA Polymerase II Pre-transcription Events / hormone-mediated signaling pathway / extracellular matrix organization / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / 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 / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / NoRC negatively regulates rRNA expression / base-excision repair / protein localization / multicellular organism growth / Dual Incision in GG-NER / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / cellular response to gamma radiation / Formation of TC-NER Pre-Incision Complex / Formation of Incision Complex in GG-NER / spindle / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / sequence-specific double-stranded DNA binding / protein-macromolecule adaptor activity / 4 iron, 4 sulfur cluster binding / 5'-3' DNA helicase activity / double-stranded DNA binding / DNA helicase / in utero embryonic development / response to oxidative stress / transcription by RNA polymerase II / damaged DNA binding 類似検索 - 分子機能 | |||||||||||||||
生物種 | Homo sapiens (ヒト) | |||||||||||||||
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 | |||||||||||||||
データ登録者 | Kokic G / Chernev A / Tegunov D / Dienemann C / Urlaub H / Cramer P | |||||||||||||||
資金援助 | ドイツ, 4件
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引用 | ジャーナル: Nat Commun / 年: 2019 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 |
ムービービューア |
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構造ビューア | EMマップ: SurfViewMolmilJmol/JSmol |
添付画像 |
-ダウンロードとリンク
-EMDBアーカイブ
マップデータ | emd_4970.map.gz | 33.9 MB | EMDBマップデータ形式 | |
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ヘッダ (付随情報) | emd-4970-v30.xml emd-4970.xml | 43.2 KB 43.2 KB | 表示 表示 | EMDBヘッダ |
FSC (解像度算出) | emd_4970_fsc_1.xml emd_4970_fsc_2.xml | 11.4 KB 11.4 KB | 表示 表示 | FSCデータファイル |
画像 | emd_4970.png | 98.3 KB | ||
マスクデータ | emd_4970_msk_1.map | 125 MB | マスクマップ | |
Filedesc metadata | emd-4970.cif.gz | 8.8 KB | ||
その他 | emd_4970_additional_1.map.gz emd_4970_additional_2.map.gz emd_4970_additional_3.map.gz emd_4970_additional_4.map.gz emd_4970_additional_5.map.gz emd_4970_additional_6.map.gz emd_4970_additional_7.map.gz emd_4970_additional_8.map.gz emd_4970_additional_9.map.gz | 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 | http://ftp.pdbj.org/pub/emdb/structures/EMD-4970 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-4970 | HTTPS FTP |
-検証レポート
文書・要旨 | emd_4970_validation.pdf.gz | 401.3 KB | 表示 | EMDB検証レポート |
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文書・詳細版 | emd_4970_full_validation.pdf.gz | 400.8 KB | 表示 | |
XML形式データ | emd_4970_validation.xml.gz | 6.3 KB | 表示 | |
CIF形式データ | emd_4970_validation.cif.gz | 7.2 KB | 表示 | |
アーカイブディレクトリ | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4970 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-4970 | HTTPS FTP |
-関連構造データ
-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_4970.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 | 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
+マスク #1
+追加マップ: Half map 1 corresponding to the composite map.
+追加マップ: Half map 2 corresponding to the composite map.
+追加マップ: Globally refined map.
+追加マップ: Half map 1 corresponding to the globally refined map.
+追加マップ: Half map 2 corresponding to the globally refined map.
+追加マップ: Focused classified and refined map using a mask...
+追加マップ: Focused classified and refined map using a mask...
+追加マップ: Focused classified and refined map using a mask...
+追加マップ: Focused classified and refined map using a mask...
-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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解析 | 単粒子再構成法 |
試料の集合状態 | particle |
-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.. |
-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: FIELD EMISSION GUN |
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 |