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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: 9sw0 | ||||||||||||||||||||||||
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| タイトル | XRCC3-RAD51C-RAD51D-XRCC2 (XRCC3 complex) capping a RAD51 filament on a D-loop intermediate | ||||||||||||||||||||||||
要素 |
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キーワード | DNA BINDING PROTEIN / complex / tumor suppresor | ||||||||||||||||||||||||
| 機能・相同性 | 機能・相同性情報telomeric loop disassembly / meiotic DNA recombinase assembly / Rad51C-XRCC3 complex / Rad51B-Rad51C-Rad51D-XRCC2 complex / double-strand break repair via synthesis-dependent strand annealing / telomere maintenance via telomere trimming / female meiosis sister chromatid cohesion / resolution of mitotic recombination intermediates / presynaptic intermediate filament cytoskeleton / response to glucoside ...telomeric loop disassembly / meiotic DNA recombinase assembly / Rad51C-XRCC3 complex / Rad51B-Rad51C-Rad51D-XRCC2 complex / double-strand break repair via synthesis-dependent strand annealing / telomere maintenance via telomere trimming / female meiosis sister chromatid cohesion / resolution of mitotic recombination intermediates / presynaptic intermediate filament cytoskeleton / response to glucoside / positive regulation of mitotic cell cycle spindle assembly checkpoint / crossover junction DNA endonuclease activity / mitotic recombination-dependent replication fork processing / DNA recombinase assembly / cellular response to camptothecin / chromosome organization involved in meiotic cell cycle / telomere maintenance via telomere lengthening / double-strand break repair involved in meiotic recombination / nuclear ubiquitin ligase complex / t-circle formation / cellular response to cisplatin / DNA strand invasion / regulation of centrosome duplication / cellular response to hydroxyurea / mitotic recombination / DNA strand exchange activity / replication-born double-strand break repair via sister chromatid exchange / lateral element / Impaired BRCA2 binding to PALB2 / regulation of DNA damage checkpoint / telomere maintenance via recombination / gamma-tubulin binding / regulation of fibroblast apoptotic process / single-stranded DNA helicase activity / reciprocal meiotic recombination / centrosome cycle / positive regulation of neurogenesis / Homologous DNA Pairing and Strand Exchange / Defective homologous recombination repair (HRR) due to BRCA1 loss of function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function / Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / sister chromatid cohesion / Resolution of D-loop Structures through Holliday Junction Intermediates / HDR through Single Strand Annealing (SSA) / ATP-dependent DNA damage sensor activity / regulation of double-strand break repair via homologous recombination / nuclear chromosome / Impaired BRCA2 binding to RAD51 / Transcriptional Regulation by E2F6 / male meiosis I / replication fork processing / microtubule organizing center / Presynaptic phase of homologous DNA pairing and strand exchange / positive regulation of G2/M transition of mitotic cell cycle / response to X-ray / ATP-dependent activity, acting on DNA / somitogenesis / interstrand cross-link repair / condensed chromosome / DNA polymerase binding / neurogenesis / telomere maintenance / replication fork / condensed nuclear chromosome / response to gamma radiation / cellular response to ionizing radiation / meiotic cell cycle / male germ cell nucleus / TP53 Regulates Transcription of DNA Repair Genes / cellular response to gamma radiation / double-strand break repair via homologous recombination / PML body / HDR through Homologous Recombination (HRR) / Meiotic recombination / response to toxic substance / multicellular organism growth / cell junction / mitotic cell cycle / single-stranded DNA binding / site of double-strand break / Factors involved in megakaryocyte development and platelet production / double-stranded DNA binding / spermatogenesis / DNA recombination / in utero embryonic development / negative regulation of neuron apoptotic process / chromosome, telomeric region / regulation of cell cycle / mitochondrial matrix / response to xenobiotic stimulus / DNA repair / intracellular membrane-bounded organelle / DNA damage response / centrosome / chromatin binding / chromatin / nucleolus / perinuclear region of cytoplasm / enzyme binding 類似検索 - 分子機能 | ||||||||||||||||||||||||
| 生物種 | Homo sapiens (ヒト)synthetic construct (人工物) | ||||||||||||||||||||||||
| 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 Å | ||||||||||||||||||||||||
データ登録者 | Greenhough, L.A. / West, S.C. | ||||||||||||||||||||||||
| 資金援助 | 英国, 4件
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引用 | ジャーナル: Science / 年: 2025タイトル: Cryo-electron microscopy visualization of RAD51 filament assembly and end-capping by XRCC3-RAD51C-RAD51D-XRCC2. 著者: Luke A Greenhough / Lorenzo Galanti / Chih-Chao Liang / Simon J Boulton / Stephen C West / ![]() 要旨: Homologous recombination repairs DNA double strand breaks and protects stalled replication forks, but how the five RAD51 paralogs contribute to these processes remains unclear. Mutations in the RAD51 ...Homologous recombination repairs DNA double strand breaks and protects stalled replication forks, but how the five RAD51 paralogs contribute to these processes remains unclear. Mutations in the RAD51 paralogs are linked to heritable breast and ovarian cancers and the cancer-prone disease Fanconi anemia. In this work, we show that the RAD51 paralogs assemble into two distinct heterotetrameric complexes, RAD51B-RAD51C-RAD51D-XRCC2 (RAD51B complex) and XRCC3-RAD51C-RAD51D-XRCC2 (XRCC3 complex). The RAD51B complex promotes dynamic adenosine triphosphate hydrolysis-dependent assembly of RAD51 filaments, whereas the XRCC3 complex stably caps the 5'-termini of RAD51 filaments to promote homologous pairing, as visualized by cryo-electron microscopy. Highly conserved across evolution, these complexes reveal insights into RAD51 filament formation and capping during DNA repair and replication fork stabilization. | ||||||||||||||||||||||||
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構造の表示
| 構造ビューア | 分子: Molmil Jmol/JSmol |
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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 | 9sw0.cif.gz | 712.1 KB | 表示 | PDBx/mmCIF形式 |
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| PDB形式 | pdb9sw0.ent.gz | 575 KB | 表示 | PDB形式 |
| PDBx/mmJSON形式 | 9sw0.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 | 9sw0_validation.pdf.gz | 2.1 MB | 表示 | wwPDB検証レポート |
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| 文書・詳細版 | 9sw0_full_validation.pdf.gz | 2.2 MB | 表示 | |
| XML形式データ | 9sw0_validation.xml.gz | 96 KB | 表示 | |
| CIF形式データ | 9sw0_validation.cif.gz | 147.9 KB | 表示 | |
| アーカイブディレクトリ | https://data.pdbj.org/pub/pdb/validation_reports/sw/9sw0 ftp://data.pdbj.org/pub/pdb/validation_reports/sw/9sw0 | HTTPS FTP |
-関連構造データ
| 関連構造データ | ![]() 55292MC ![]() 9svxC ![]() 9svyC 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 F&H 検索 |
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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 repair protein ... , 5種, 11分子 BFGEHIJKACD
| #1: タンパク質 | 分子量: 35084.254 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: RAD51D, RAD51L3発現宿主: ![]() 参照: UniProt: O75771 | ||||||
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| #2: タンパク質 | 分子量: 37009.125 Da / 分子数: 7 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: RAD51, RAD51A, RECA / 発現宿主: ![]() #6: タンパク質 | | 分子量: 31995.525 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: XRCC2発現宿主: ![]() 参照: UniProt: O43543 #7: タンパク質 | | 分子量: 42244.609 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: RAD51C, RAD51L2発現宿主: ![]() 参照: UniProt: O43502 #8: タンパク質 | | 分子量: 37899.781 Da / 分子数: 1 / 由来タイプ: 組換発現 / 由来: (組換発現) Homo sapiens (ヒト) / 遺伝子: XRCC3発現宿主: ![]() 参照: UniProt: O43542 |
-DNA鎖 , 3種, 3分子 MNO
| #3: DNA鎖 | 分子量: 9460.064 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) synthetic construct (人工物) |
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| #4: DNA鎖 | 分子量: 18211.734 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) synthetic construct (人工物) |
| #5: DNA鎖 | 分子量: 17969.551 Da / 分子数: 1 / 由来タイプ: 合成 / 由来: (合成) synthetic construct (人工物) |
-非ポリマー , 4種, 24分子 






| #9: 化合物 | ChemComp-ATP / #10: 化合物 | ChemComp-CA / #11: 化合物 | ChemComp-MG / #12: 化合物 | ChemComp-ADP / | |
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-詳細
| 研究の焦点であるリガンドがあるか | Y |
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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: XRCC3-RAD51C-RAD51D-XRCC2 (XRCC3 complex) capping a RAD51 filament on a D-loop intermediate タイプ: COMPLEX / Entity ID: #1-#8 / 由来: RECOMBINANT | |||||||||||||||||||||||||||||||||||
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| 分子量 | 実験値: NO | |||||||||||||||||||||||||||||||||||
| 由来(天然) | 生物種: Homo sapiens (ヒト) | |||||||||||||||||||||||||||||||||||
| 由来(組換発現) | 生物種: ![]() 株: Sf9 | |||||||||||||||||||||||||||||||||||
| 緩衝液 | pH: 7.5 詳細: 25 mM HEPES-NaOH pH 7.5, 100 mM NaCl, 2.5 mM MgCl2, 2.5 mM CaCl2, 1 mM ATP, 0.25 mM TCEP | |||||||||||||||||||||||||||||||||||
| 緩衝液成分 |
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| 試料 | 包埋: NO / シャドウイング: NO / 染色: NO / 凍結: YES | |||||||||||||||||||||||||||||||||||
| 急速凍結 | 装置: FEI VITROBOT MARK IV / 凍結剤: ETHANE / 湿度: 95 % / 凍結前の試料温度: 277 K |
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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: TFS KRIOS |
| 電子銃 | 電子線源: FIELD EMISSION GUN / 加速電圧: 300 kV / 照射モード: SPOT SCAN |
| 電子レンズ | モード: BRIGHT FIELD / 倍率(公称値): 130000 X / 最大 デフォーカス(公称値): 2300 nm / 最小 デフォーカス(公称値): 800 nm |
| 試料ホルダ | 凍結剤: NITROGEN 試料ホルダーモデル: FEI TITAN KRIOS AUTOGRID HOLDER |
| 撮影 | 電子線照射量: 48.4 e/Å2 フィルム・検出器のモデル: FEI FALCON IV (4k x 4k) |
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解析
| EMソフトウェア |
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| CTF補正 | タイプ: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
| 粒子像の選択 | 選択した粒子像数: 35223698 | ||||||||||||||||||||||||
| 3次元再構成 | 解像度: 3 Å / 解像度の算出法: FSC 0.143 CUT-OFF / 粒子像の数: 29848 / 対称性のタイプ: POINT | ||||||||||||||||||||||||
| 精密化 | 最高解像度: 3 Å / 交差検証法: NONE 立体化学のターゲット値: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| 拘束条件 |
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ムービー
コントローラー
万見について




Homo sapiens (ヒト)
英国, 4件
引用




PDBj

















































FIELD EMISSION GUN