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基本情報
登録情報 | データベース: PDB / ID: 8b3g | |||||||||||||||||||||
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タイトル | C(N)RL4CSA-UVSSA-E2-ubiquitin complex. | |||||||||||||||||||||
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![]() | TRANSCRIPTION / DNA repair / ubiquitin / cryo-EM | |||||||||||||||||||||
機能・相同性 | ![]() RNA polymerase inhibitor activity / regulation of transcription-coupled nucleotide-excision repair / nucleotide-excision repair complex / negative regulation of granulocyte differentiation / cullin-RING-type E3 NEDD8 transferase / NEDD8 transferase activity / cullin-RING ubiquitin ligase complex / single strand break repair / cellular response to chemical stress / regulation of DNA damage checkpoint ...RNA polymerase inhibitor activity / regulation of transcription-coupled nucleotide-excision repair / nucleotide-excision repair complex / negative regulation of granulocyte differentiation / cullin-RING-type E3 NEDD8 transferase / NEDD8 transferase activity / cullin-RING ubiquitin ligase complex / single strand break repair / cellular response to chemical stress / regulation of DNA damage checkpoint / positive regulation by virus of viral protein levels in host cell / Cul7-RING ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / chromatin-protein adaptor activity / double-strand break repair via classical nonhomologous end joining / Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling / spindle assembly involved in female meiosis / regulation of nucleotide-excision repair / epigenetic programming in the zygotic pronuclei / Cul4-RING E3 ubiquitin ligase complex / positive regulation of protein autoubiquitination / protein neddylation / UV-damage excision repair / NEDD8 ligase activity / negative regulation of response to oxidative stress / Cul5-RING ubiquitin ligase complex / biological process involved in interaction with symbiont / regulation of mitotic cell cycle phase transition / SCF ubiquitin ligase complex / WD40-repeat domain binding / Cul2-RING ubiquitin ligase complex / ubiquitin-ubiquitin ligase activity / Cul4A-RING E3 ubiquitin ligase complex / negative regulation of type I interferon production / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / Cul3-RING ubiquitin ligase complex / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / negative regulation of mitophagy / Prolactin receptor signaling / negative regulation of reproductive process / negative regulation of developmental process / TGF-beta receptor signaling activates SMADs / RNA polymerase II complex binding / cullin family protein binding / viral release from host cell / hemopoiesis / site of DNA damage / regulation of proteolysis / regulation of postsynapse assembly / somatic stem cell population maintenance / anatomical structure morphogenesis / protein monoubiquitination / response to X-ray / ectopic germ cell programmed cell death / positive regulation of G1/S transition of mitotic cell cycle / positive regulation of viral genome replication / protein K48-linked ubiquitination / proteasomal protein catabolic process / transcription-coupled nucleotide-excision repair / response to UV / protein autoubiquitination / Nuclear events stimulated by ALK signaling in cancer / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / regulation of cellular response to insulin stimulus / FLT3 signaling by CBL mutants / positive regulation of gluconeogenesis / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / positive regulation of TORC1 signaling / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / Constitutive Signaling by NOTCH1 HD Domain Mutants / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / post-translational protein modification / APC-Cdc20 mediated degradation of Nek2A / p75NTR recruits signalling complexes / intrinsic apoptotic signaling pathway / InlA-mediated entry of Listeria monocytogenes into host cells / negative regulation of insulin receptor signaling pathway / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism 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: 4.4 Å | |||||||||||||||||||||
![]() | Kokic, G. / Cramer, P. | |||||||||||||||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structural basis for RNA polymerase II ubiquitylation and inactivation in transcription-coupled repair. 著者: Goran Kokic / George Yakoub / Diana van den Heuvel / Annelotte P Wondergem / Paula J van der Meer / Yana van der Weegen / Aleksandar Chernev / Isaac Fianu / Thornton J Fokkens / Sonja Lorenz ...著者: Goran Kokic / George Yakoub / Diana van den Heuvel / Annelotte P Wondergem / Paula J van der Meer / Yana van der Weegen / Aleksandar Chernev / Isaac Fianu / Thornton J Fokkens / Sonja Lorenz / Henning Urlaub / Patrick Cramer / Martijn S Luijsterburg / ![]() ![]() 要旨: During transcription-coupled DNA repair (TCR), RNA polymerase II (Pol II) transitions from a transcriptionally active state to an arrested state that allows for removal of DNA lesions. This ...During transcription-coupled DNA repair (TCR), RNA polymerase II (Pol II) transitions from a transcriptionally active state to an arrested state that allows for removal of DNA lesions. This transition requires site-specific ubiquitylation of Pol II by the CRL4 ubiquitin ligase, a process that is facilitated by ELOF1 in an unknown way. Using cryogenic electron microscopy, biochemical assays and cell biology approaches, we found that ELOF1 serves as an adaptor to stably position UVSSA and CRL4 on arrested Pol II, leading to ligase neddylation and activation of Pol II ubiquitylation. In the presence of ELOF1, a transcription factor IIS (TFIIS)-like element in UVSSA gets ordered and extends through the Pol II pore, thus preventing reactivation of Pol II by TFIIS. Our results provide the structural basis for Pol II ubiquitylation and inactivation in TCR. | |||||||||||||||||||||
履歴 |
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構造の表示
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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ダウンロード
PDBx/mmCIF形式 | ![]() | 907.3 KB | 表示 | ![]() |
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PDB形式 | ![]() | 744.1 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 | ![]() | 1.2 MB | 表示 | ![]() |
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文書・詳細版 | ![]() | 1.2 MB | 表示 | |
XML形式データ | ![]() | 77 KB | 表示 | |
CIF形式データ | ![]() | 118.6 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 | ![]() 15827MC 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 | 類似検索 - 機能・相同性 ![]() |
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リンク
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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 , 8種, 8分子 DNRUacde
#1: タンパク質 | 分子量: 16755.227 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() |
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#2: タンパク質 | 分子量: 8573.978 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() ![]() |
#3: タンパク質 | 分子量: 12289.977 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) ![]() ![]() 参照: UniProt: P62877, RING-type E3 ubiquitin transferase, cullin-RING-type E3 NEDD8 transferase |
#4: タンパク質 | 分子量: 8576.831 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: 44107.160 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: 80721.680 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: 127097.469 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: 87814.297 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 , 1種, 3分子 
#9: 化合物 |
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-詳細
研究の焦点であるリガンドがあるか | N |
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Has protein modification | N |
-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: C(N)RL4CSA-UVSSA-E2-ubiquitin complex. / タイプ: COMPLEX / Entity ID: #1-#8 / 由来: RECOMBINANT |
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由来(天然) | 生物種: ![]() |
由来(組換発現) | 生物種: ![]() |
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
顕微鏡 | モデル: TFS GLACIOS |
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電子銃 | 電子線源: ![]() |
電子レンズ | モード: BRIGHT FIELD / 最大 デフォーカス(公称値): 3550 nm / 最小 デフォーカス(公称値): 400 nm |
撮影 | 電子線照射量: 40.2 e/Å2 フィルム・検出器のモデル: FEI FALCON III (4k x 4k) |
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解析
ソフトウェア | 名称: PHENIX / バージョン: 1.18.2_3874: / 分類: 精密化 | ||||||||||||||||||||||||
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EMソフトウェア | 名称: PHENIX / カテゴリ: モデル精密化 | ||||||||||||||||||||||||
CTF補正 | タイプ: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3次元再構成 | 解像度: 4.4 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 67365 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
拘束条件 |
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