+データを開く
-基本情報
登録情報 | データベース: PDB / ID: 5yz0 | ||||||||||||||||||||||||
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タイトル | Cryo-EM Structure of human ATR-ATRIP complex | ||||||||||||||||||||||||
要素 |
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キーワード | CELL CYCLE / cryo-EM / ATR-ATRIP / DNA damnage response | ||||||||||||||||||||||||
機能・相同性 | 機能・相同性情報 ATR-ATRIP complex / establishment of RNA localization to telomere / positive regulation of telomerase catalytic core complex assembly / MutSalpha complex binding / positive regulation of DNA damage response, signal transduction by p53 class mediator / establishment of protein-containing complex localization to telomere / response to xenobiotic stimulus => GO:0009410 / multicellular organism development / MutLalpha complex binding / regulation of double-strand break repair ...ATR-ATRIP complex / establishment of RNA localization to telomere / positive regulation of telomerase catalytic core complex assembly / MutSalpha complex binding / positive regulation of DNA damage response, signal transduction by p53 class mediator / establishment of protein-containing complex localization to telomere / response to xenobiotic stimulus => GO:0009410 / multicellular organism development / MutLalpha complex binding / regulation of double-strand break repair / nucleobase-containing compound metabolic process / HDR through Single Strand Annealing (SSA) / protein localization to chromosome, telomeric region / Impaired BRCA2 binding to RAD51 / K63-linked polyubiquitin modification-dependent protein binding / negative regulation of DNA replication / Presynaptic phase of homologous DNA pairing and strand exchange / replicative senescence / Regulation of HSF1-mediated heat shock response / Activation of ATR in response to replication stress / interstrand cross-link repair / regulation of cellular response to heat / positive regulation of telomere maintenance via telomerase / Meiotic synapsis / telomere maintenance / regulation of signal transduction by p53 class mediator / DNA damage checkpoint signaling / Fanconi Anemia Pathway / TP53 Regulates Transcription of DNA Repair Genes / G2/M DNA damage checkpoint / cellular response to gamma radiation / PML body / cellular response to UV / chromosome / Processing of DNA double-strand break ends / peptidyl-serine phosphorylation / DNA replication / Regulation of TP53 Activity through Phosphorylation / protein autophosphorylation / non-specific serine/threonine protein kinase / protein kinase activity / DNA repair / protein serine/threonine kinase activity / DNA damage response / Golgi apparatus / DNA binding / nucleoplasm / ATP binding / nucleus 類似検索 - 分子機能 | ||||||||||||||||||||||||
生物種 | Homo sapiens (ヒト) | ||||||||||||||||||||||||
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: 4.7 Å | ||||||||||||||||||||||||
データ登録者 | Rao, Q. / Liu, M. / Tian, Y. / Wu, Z. / Wang, H. / Wang, J. / Xu, Y. | ||||||||||||||||||||||||
資金援助 | 中国, 7件
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引用 | ジャーナル: Cell Res / 年: 2018 タイトル: Cryo-EM structure of human ATR-ATRIP complex. 著者: Qinhui Rao / Mengjie Liu / Yuan Tian / Zihan Wu / Yuhan Hao / Lei Song / Zhaoyu Qin / Chen Ding / Hong-Wei Wang / Jiawei Wang / Yanhui Xu / 要旨: ATR (ataxia telangiectasia-mutated and Rad3-related) protein kinase and ATRIP (ATR-interacting protein) form a complex and play a critical role in response to replication stress and DNA damage. Here, ...ATR (ataxia telangiectasia-mutated and Rad3-related) protein kinase and ATRIP (ATR-interacting protein) form a complex and play a critical role in response to replication stress and DNA damage. Here, we determined the cryo-electron microscopy (EM) structure of the human ATR-ATRIP complex at 4.7 Å resolution and built an atomic model of the C-terminal catalytic core of ATR (residues 1 521-2 644) at 3.9 Å resolution. The complex adopts a hollow "heart" shape, consisting of two ATR monomers in distinct conformations. The EM map for ATRIP reveals 14 HEAT repeats in an extended "S" shape. The conformational flexibility of ATR allows ATRIP to properly lock the N-termini of the two ATR monomers to favor ATR-ATRIP complex formation and functional diversity. The isolated "head-head" and "tail-tail" each adopts a pseudo 2-fold symmetry. The catalytic pockets face outward and substrate access is not restricted by inhibitory elements. Our studies provide a structural basis for understanding the assembly of the ATR-ATRIP complex and a framework for characterizing ATR-mediated DNA repair pathways. | ||||||||||||||||||||||||
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 | 分子: MolmilJmol/JSmol |
-ダウンロードとリンク
-ダウンロード
PDBx/mmCIF形式 | 5yz0.cif.gz | 845.8 KB | 表示 | PDBx/mmCIF形式 |
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PDB形式 | pdb5yz0.ent.gz | 639.6 KB | 表示 | PDB形式 |
PDBx/mmJSON形式 | 5yz0.json.gz | ツリー表示 | PDBx/mmJSON形式 | |
その他 | その他のダウンロード |
-検証レポート
文書・要旨 | 5yz0_validation.pdf.gz | 806.7 KB | 表示 | wwPDB検証レポート |
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文書・詳細版 | 5yz0_full_validation.pdf.gz | 917.2 KB | 表示 | |
XML形式データ | 5yz0_validation.xml.gz | 130.6 KB | 表示 | |
CIF形式データ | 5yz0_validation.cif.gz | 209.6 KB | 表示 | |
アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/yz/5yz0 ftp://data.pdbj.org/pub/pdb/validation_reports/yz/5yz0 | HTTPS FTP |
-関連構造データ
-リンク
-集合体
登録構造単位 |
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-要素
#1: タンパク質 | 分子量: 301756.781 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: ATR, FRP1 / 細胞株 (発現宿主): 293F / 発現宿主: Homo sapiens (ヒト) 参照: UniProt: Q13535, non-specific serine/threonine protein kinase #2: タンパク質 | 分子量: 85940.664 Da / 分子数: 2 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: ATRIP, AGS1 / 細胞株 (発現宿主): 293F / 発現宿主: Homo sapiens (ヒト) / 参照: UniProt: Q8WXE1 |
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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 |
-試料調製
構成要素 | 名称: ATR-ATRIP complex / タイプ: COMPLEX / Entity ID: all / 由来: RECOMBINANT |
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分子量 | 値: 700 kDa/nm / 実験値: YES |
由来(天然) | 生物種: Homo sapiens (ヒト) |
由来(組換発現) | 生物種: Homo sapiens (ヒト) / 細胞: 293F |
緩衝液 | pH: 7.4 |
試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES |
試料支持 | グリッドの材料: GOLD / グリッドのサイズ: 300 divisions/in. / グリッドのタイプ: Quantifoil R1.2/1.3 |
急速凍結 | 凍結剤: ETHANE |
-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: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: FLOOD BEAM |
電子レンズ | モード: BRIGHT FIELD |
撮影 | 電子線照射量: 50 e/Å2 / 検出モード: SUPER-RESOLUTION フィルム・検出器のモデル: GATAN K2 SUMMIT (4k x 4k) |
画像スキャン | 動画フレーム数/画像: 32 / 利用したフレーム数/画像: 1-32 |
-解析
ソフトウェア | 名称: PHENIX / バージョン: 1.12_2829: / 分類: 精密化 | ||||||||||||||||||||||||
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CTF補正 | タイプ: NONE | ||||||||||||||||||||||||
3次元再構成 | 解像度: 4.7 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 266218 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
拘束条件 |
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