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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: 7ad8 | ||||||
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タイトル | Core TFIIH-XPA-DNA complex with modelled p62 subunit | ||||||
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![]() | DNA BINDING PROTEIN / DNA repair / transcription factor | ||||||
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 / spinal cord development / erythrocyte maturation / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / hematopoietic stem cell proliferation / 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 / Formation of HIV elongation complex in the absence of HIV Tat / transcription elongation by RNA polymerase I / 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 / RNA Polymerase I Promoter Escape / transcription elongation by RNA polymerase II / 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 / NoRC negatively regulates rRNA expression / base-excision repair / 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 | 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: 3.5 Å | ||||||
![]() | Koelmel, W. / Kuper, J. / Kisker, C. | ||||||
資金援助 | ![]()
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![]() | ![]() タイトル: The TFIIH subunits p44/p62 act as a damage sensor during nucleotide excision repair. 著者: Jamie T Barnett / Jochen Kuper / Wolfgang Koelmel / Caroline Kisker / Neil M Kad / ![]() ![]() 要旨: Nucleotide excision repair (NER) in eukaryotes is orchestrated by the core form of the general transcription factor TFIIH, containing the helicases XPB, XPD and five 'structural' subunits, p62, p44, ...Nucleotide excision repair (NER) in eukaryotes is orchestrated by the core form of the general transcription factor TFIIH, containing the helicases XPB, XPD and five 'structural' subunits, p62, p44, p34, p52 and p8. Recent cryo-EM structures show that p62 makes extensive contacts with p44 and in part occupies XPD's DNA binding site. While p44 is known to regulate the helicase activity of XPD during NER, p62 is thought to be purely structural. Here, using helicase and adenosine triphosphatase assays we show that a complex containing p44 and p62 enhances XPD's affinity for dsDNA 3-fold over p44 alone. Remarkably, the relative affinity is further increased to 60-fold by dsDNA damage. Direct binding studies show this preference derives from p44/p62's high affinity (20 nM) for damaged ssDNA. Single molecule imaging of p44/p62 complexes without XPD reveals they bind to and randomly diffuse on DNA, however, in the presence of UV-induced DNA lesions these complexes stall. Combined with the analysis of a recent cryo-EM structure, we suggest that p44/p62 acts as a novel DNA-binding entity that enhances damage recognition in TFIIH. This revises our understanding of TFIIH and prompts investigation into the core subunits for an active role during DNA repair and/or transcription. | ||||||
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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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ダウンロードとリンク
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PDBx/mmCIF形式 | ![]() | 505.5 KB | 表示 | ![]() |
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PDB形式 | ![]() | 390.9 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 | ![]() | 808.6 KB | 表示 | ![]() |
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文書・詳細版 | ![]() | 823.2 KB | 表示 | |
XML形式データ | ![]() | 67.1 KB | 表示 | |
CIF形式データ | ![]() | 104.4 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 | ![]() 4970M M: このデータのモデリングに利用したマップデータ |
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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
-DNA鎖 , 2種, 2分子 JK
#1: DNA鎖 | 分子量: 15036.663 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) ![]() |
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#2: DNA鎖 | 分子量: 15075.698 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) ![]() |
-タンパク質 , 3種, 3分子 ABG
#3: 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) ![]() ![]() |
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#5: 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) ![]() ![]() |
#9: タンパク質 | 分子量: 31422.053 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
-General transcription factor IIH subunit ... , 5種, 5分子 FEDCI
#4: 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) ![]() ![]() |
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#6: 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) ![]() ![]() |
#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: 52245.156 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() |
#10: 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) ![]() ![]() |
-非ポリマー , 2種, 7分子 


#11: 化合物 | ChemComp-SF4 / |
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#12: 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 |
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分子量 | 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 | ||||||||||||||||||||||||
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 e/Å2 フィルム・検出器のモデル: GATAN K2 SUMMIT (4k 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: 3.5 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 227776 / 対称性のタイプ: POINT |