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データを開く
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基本情報
登録情報 | ![]() | |||||||||
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タイトル | Structure of DNA-bound human RAD17-RFC clamp loader and 9-1-1 checkpoint clamp | |||||||||
![]() | Map | |||||||||
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機能・相同性 | ![]() meiotic DNA integrity checkpoint signaling / checkpoint clamp complex / meiotic recombination checkpoint signaling / Rad17 RFC-like complex / Elg1 RFC-like complex / DNA replication factor C complex / Ctf18 RFC-like complex / double-stranded DNA 3'-5' DNA exonuclease activity / exodeoxyribonuclease III / DNA clamp loader activity ...meiotic DNA integrity checkpoint signaling / checkpoint clamp complex / meiotic recombination checkpoint signaling / Rad17 RFC-like complex / Elg1 RFC-like complex / DNA replication factor C complex / Ctf18 RFC-like complex / double-stranded DNA 3'-5' DNA exonuclease activity / exodeoxyribonuclease III / DNA clamp loader activity / positive regulation of DNA-directed DNA polymerase activity / DNA replication checkpoint signaling / Polymerase switching / chromatin-protein adaptor activity / regulation of phosphorylation / protein localization to site of double-strand break / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / mitotic DNA replication checkpoint signaling / Polymerase switching on the C-strand of the telomere / mitotic intra-S DNA damage checkpoint signaling / embryo development ending in birth or egg hatching / HDR through Single Strand Annealing (SSA) / Impaired BRCA2 binding to RAD51 / DNA synthesis involved in DNA repair / DNA strand elongation involved in DNA replication / negative regulation of DNA replication / Presynaptic phase of homologous DNA pairing and strand exchange / PCNA-Dependent Long Patch Base Excision Repair / ATP-dependent activity, acting on DNA / Activation of ATR in response to replication stress / response to UV / 3'-5' exonuclease activity / substantia nigra development / telomere maintenance / DNA damage checkpoint signaling / Translesion synthesis by REV1 / Translesion synthesis by POLK / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / cellular response to ionizing radiation / nucleotide-excision repair / Termination of translesion DNA synthesis / Recognition of DNA damage by PCNA-containing replication complex / double-strand break repair via homologous recombination / Translesion Synthesis by POLH / G2/M DNA damage checkpoint / HDR through Homologous Recombination (HRR) / SH3 domain binding / Dual Incision in GG-NER / DNA-templated DNA replication / histone deacetylase binding / intrinsic apoptotic signaling pathway in response to DNA damage / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / site of double-strand break / chromosome / Processing of DNA double-strand break ends / Regulation of TP53 Activity through Phosphorylation / damaged DNA binding / DNA replication / DNA repair / intracellular membrane-bounded organelle / DNA damage response / chromatin binding / protein kinase binding / nucleolus / enzyme binding / ATP hydrolysis activity / DNA binding / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm 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: 3.59 Å | |||||||||
![]() | Day M / Oliver AW / Pearl LH | |||||||||
資金援助 | ![]()
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![]() | ![]() タイトル: Structure of the human RAD17-RFC clamp loader and 9-1-1 checkpoint clamp bound to a dsDNA-ssDNA junction. 著者: Matthew Day / Antony W Oliver / Laurence H Pearl / ![]() 要旨: The RAD9-RAD1-HUS1 (9-1-1) clamp forms one half of the DNA damage checkpoint system that signals the presence of substantial regions of single-stranded DNA arising from replication fork collapse or ...The RAD9-RAD1-HUS1 (9-1-1) clamp forms one half of the DNA damage checkpoint system that signals the presence of substantial regions of single-stranded DNA arising from replication fork collapse or resection of DNA double strand breaks. Loaded at the 5'-recessed end of a dsDNA-ssDNA junction by the RAD17-RFC clamp loader complex, the phosphorylated C-terminal tail of the RAD9 subunit of 9-1-1 engages with the mediator scaffold TOPBP1 which in turn activates the ATR kinase, localised through the interaction of its constitutive partner ATRIP with RPA-coated ssDNA. Using cryogenic electron microscopy (cryoEM) we have determined the structure of a complex of the human RAD17-RFC clamp loader bound to human 9-1-1, engaged with a dsDNA-ssDNA junction. The structure answers the key questions of how RAD17 confers specificity for 9-1-1 over PCNA, and how the clamp loader specifically recognises the recessed 5' DNA end and fixes the orientation of 9-1-1 on the ssDNA. | |||||||||
履歴 |
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構造の表示
添付画像 |
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ダウンロードとリンク
-EMDBアーカイブ
マップデータ | ![]() | 87.6 MB | ![]() | |
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ヘッダ (付随情報) | ![]() ![]() | 24.8 KB 24.8 KB | 表示 表示 | ![]() |
FSC (解像度算出) | ![]() | 10.6 KB | 表示 | ![]() |
画像 | ![]() | 113.7 KB | ||
その他 | ![]() ![]() | 77.4 MB 77.4 MB | ||
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 | ![]() 7z6hMC M: このマップから作成された原子モデル 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 ![]() |
電子顕微鏡画像生データ | ![]() Data size: 4.4 TB Data #1: unaligned multiframe EER movies for human RAD17-RFC clamp loader and 9-1-1 checkpoint clamp bound to a dsDNA-ssDNA junction [micrographs - multiframe]) |
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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 | Map | ||||||||||||||||||||||||||||||||||||
投影像・断面図 | 画像のコントロール
画像は Spider により作成 | ||||||||||||||||||||||||||||||||||||
ボクセルのサイズ | X=Y=Z: 0.86 Å | ||||||||||||||||||||||||||||||||||||
密度 |
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対称性 | 空間群: 1 | ||||||||||||||||||||||||||||||||||||
詳細 | EMDB XML:
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-添付データ
-ハーフマップ: Half-map 1
ファイル | emd_14527_half_map_1.map | ||||||||||||
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注釈 | Half-map 1 | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
-ハーフマップ: Half-map 2
ファイル | emd_14527_half_map_2.map | ||||||||||||
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注釈 | Half-map 2 | ||||||||||||
投影像・断面図 |
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密度ヒストグラム |
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試料の構成要素
+全体 : DNA-bound human RAD17-RFC clamp loader and 9-1-1 checkpoint clamp
+超分子 #1: DNA-bound human RAD17-RFC clamp loader and 9-1-1 checkpoint clamp
+分子 #1: Cell cycle checkpoint control protein RAD9A
+分子 #2: Cell cycle checkpoint protein RAD1,Cell cycle checkpoint protein RAD17
+分子 #3: Checkpoint protein HUS1
+分子 #4: Replication factor C subunit 4
+分子 #5: Replication factor C subunit 3
+分子 #6: Replication factor C subunit 2
+分子 #7: Replication factor C subunit 5
+分子 #8: Hairpin DNA
+分子 #9: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
-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
濃度 | 0.21 mg/mL |
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緩衝液 | pH: 7.5 |
グリッド | モデル: Quantifoil R1.2/1.3 / 材質: COPPER / 前処理 - タイプ: PLASMA CLEANING |
凍結 | 凍結剤: ETHANE-PROPANE |
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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: FEI FALCON IV (4k x 4k) 平均電子線量: 34.9 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: OTHER / 最大 デフォーカス(公称値): 2.5 µm / 最小 デフォーカス(公称値): 1.5 µm |
実験機器 | ![]() モデル: Titan Krios / 画像提供: FEI Company |