- EMDB-28961: Cryo-EM structure of the human BCDX2 complex -
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基本情報
登録情報
データベース: EMDB / ID: EMD-28961
タイトル
Cryo-EM structure of the human BCDX2 complex
マップデータ
EM map, MRC format.
試料
複合体: Cryo-EM structure of the human heterotetrameric BCDX2 complex
タンパク質・ペプチド: DNA repair protein RAD51 homolog 2
タンパク質・ペプチド: DNA repair protein RAD51 homolog 3
タンパク質・ペプチド: DNA repair protein RAD51 homolog 4
タンパク質・ペプチド: DNA repair protein XRCC2
リガンド: ADENOSINE-5'-DIPHOSPHATE
リガンド: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
リガンド: MAGNESIUM ION
キーワード
DNA binding protein / ATP binding domain / homologous recombination / RAD51 paralog / RECOMBINATION
機能・相同性
機能・相同性情報
meiotic DNA recombinase assembly / Rad51C-XRCC3 complex / Rad51B-Rad51C-Rad51D-XRCC2 complex / female meiosis sister chromatid cohesion / blastocyst growth / crossover junction DNA endonuclease activity / somite development / telomere maintenance via recombination / Impaired BRCA2 binding to PALB2 / DNA strand invasion ...meiotic DNA recombinase assembly / Rad51C-XRCC3 complex / Rad51B-Rad51C-Rad51D-XRCC2 complex / female meiosis sister chromatid cohesion / blastocyst growth / crossover junction DNA endonuclease activity / somite development / telomere maintenance via recombination / Impaired BRCA2 binding to PALB2 / DNA strand invasion / gamma-tubulin binding / reciprocal meiotic recombination / sister chromatid cohesion / regulation of fibroblast apoptotic process / centrosome cycle / 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 / Homologous DNA Pairing and Strand Exchange / Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA) / Resolution of D-loop Structures through Holliday Junction Intermediates / positive regulation of neurogenesis / ATP-dependent DNA damage sensor activity / male meiosis I / Presynaptic phase of homologous DNA pairing and strand exchange / response to X-ray / ATP-dependent activity, acting on DNA / somitogenesis / interstrand cross-link repair / four-way junction DNA binding / positive regulation of G2/M transition of mitotic cell cycle / telomere maintenance / neurogenesis / meiotic cell cycle / replication fork / response to gamma radiation / TP53 Regulates Transcription of DNA Repair Genes / double-strand break repair via homologous recombination / HDR through Homologous Recombination (HRR) / multicellular organism growth / Meiotic recombination / cell junction / mitotic cell cycle / single-stranded DNA binding / Factors involved in megakaryocyte development and platelet production / spermatogenesis / double-stranded DNA binding / DNA recombination / in utero embryonic development / negative regulation of neuron apoptotic process / chromosome, telomeric region / regulation of cell cycle / intracellular membrane-bounded organelle / DNA repair / centrosome / positive regulation of cell population proliferation / perinuclear region of cytoplasm / ATP hydrolysis activity / mitochondrion / DNA binding / nucleoplasm / ATP binding / nucleus / cytoplasm / cytosol 類似検索 - 分子機能
DNA repair protein XRCC2 / DNA repair protein RAD51 homologue 2 / : / : / RAD51D, N-terminal domain / DNA recombination and repair protein, RecA-like / DNA recombination and repair protein Rad51-like, C-terminal / Rad51 / DNA recombination and repair protein RecA-like, ATP-binding domain / RecA family profile 1. ...DNA repair protein XRCC2 / DNA repair protein RAD51 homologue 2 / : / : / RAD51D, N-terminal domain / DNA recombination and repair protein, RecA-like / DNA recombination and repair protein Rad51-like, C-terminal / Rad51 / DNA recombination and repair protein RecA-like, ATP-binding domain / RecA family profile 1. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性
DNA repair protein RAD51 homolog 2 / DNA repair protein RAD51 homolog 3 / DNA repair protein XRCC2 / DNA repair protein RAD51 homolog 4 類似検索 - 構成要素
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01 GM115568
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R01 GM128731
米国
Cancer Prevention and Research Institute of Texas (CPRIT)
RR200030
米国
National Institutes of Health/National Cancer Institute (NIH/NCI)
R01 CA168635
米国
National Institutes of Health/National Cancer Institute (NIH/NCI)
R35 CA241801
米国
Cancer Prevention and Research Institute of Texas (CPRIT)
RR180029
米国
Cancer Prevention and Research Institute of Texas (CPRIT)
RR210023
米国
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R00 GM140264
米国
Cancer Prevention and Research Institute of Texas (CPRIT)
RR220068
米国
引用
ジャーナル: Nature / 年: 2023 タイトル: Structural insights into BCDX2 complex function in homologous recombination. 著者: Yashpal Rawal / Lijia Jia / Aviv Meir / Shuo Zhou / Hardeep Kaur / Eliza A Ruben / Youngho Kwon / Kara A Bernstein / Maria Jasin / Alexander B Taylor / Sandeep Burma / Robert Hromas / ...著者: Yashpal Rawal / Lijia Jia / Aviv Meir / Shuo Zhou / Hardeep Kaur / Eliza A Ruben / Youngho Kwon / Kara A Bernstein / Maria Jasin / Alexander B Taylor / Sandeep Burma / Robert Hromas / Alexander V Mazin / Weixing Zhao / Daohong Zhou / Elizabeth V Wasmuth / Eric C Greene / Patrick Sung / Shaun K Olsen / 要旨: Homologous recombination (HR) fulfils a pivotal role in the repair of DNA double-strand breaks and collapsed replication forks. HR depends on the products of several paralogues of RAD51, including ...Homologous recombination (HR) fulfils a pivotal role in the repair of DNA double-strand breaks and collapsed replication forks. HR depends on the products of several paralogues of RAD51, including the tetrameric complex of RAD51B, RAD51C, RAD51D and XRCC2 (BCDX2). BCDX2 functions as a mediator of nucleoprotein filament assembly by RAD51 and single-stranded DNA (ssDNA) during HR, but its mechanism remains undefined. Here we report cryogenic electron microscopy reconstructions of human BCDX2 in apo and ssDNA-bound states. The structures reveal how the amino-terminal domains of RAD51B, RAD51C and RAD51D participate in inter-subunit interactions that underpin complex formation and ssDNA-binding specificity. Single-molecule DNA curtain analysis yields insights into how BCDX2 enhances RAD51-ssDNA nucleoprotein filament assembly. Moreover, our cryogenic electron microscopy and functional analyses explain how RAD51C alterations found in patients with cancer inactivate DNA binding and the HR mediator activity of BCDX2. Our findings shed light on the role of BCDX2 in HR and provide a foundation for understanding how pathogenic alterations in BCDX2 impact genome repair.