- EMDB-15805: RecBCD-DNA in complex with the phage protein Abc2 and host PpiB -
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基本情報
登録情報
データベース: EMDB / ID: EMD-15805
タイトル
RecBCD-DNA in complex with the phage protein Abc2 and host PpiB
マップデータ
Final CryoEM map of the RecBCD-Abc2-DNA complex bound to the host PpiB protein
試料
複合体: RecBCD-Abc2-PpiB-DNA complex
複合体: RecBCD enzyme subunits RecB, RecC and RecD
タンパク質・ペプチド: RecBCD enzyme subunit RecB
タンパク質・ペプチド: RecBCD enzyme subunit RecC
タンパク質・ペプチド: RecBCD enzyme subunit RecD
複合体: DNA (70-MER)
DNA: DNA (70-MER)
複合体: Anti-RecBCD protein 2
タンパク質・ペプチド: Anti-RecBCD protein 2
リガンド: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
リガンド: MAGNESIUM ION
キーワード
Homologous recombination / DNA repair / phage / Helicase / Nuclease / Inhibitor / Protein complex / Enzyme / DNA mimic / DNA BINDING PROTEIN
機能・相同性
機能・相同性情報
exodeoxyribonuclease V / exodeoxyribonuclease V activity / exodeoxyribonuclease V complex / clearance of foreign intracellular DNA / DNA 5'-3' helicase / DNA 3'-5' helicase / recombinational repair / single-stranded DNA helicase activity / 3'-5' DNA helicase activity / DNA helicase activity ...exodeoxyribonuclease V / exodeoxyribonuclease V activity / exodeoxyribonuclease V complex / clearance of foreign intracellular DNA / DNA 5'-3' helicase / DNA 3'-5' helicase / recombinational repair / single-stranded DNA helicase activity / 3'-5' DNA helicase activity / DNA helicase activity / isomerase activity / helicase activity / double-strand break repair via homologous recombination / response to radiation / 5'-3' DNA helicase activity / DNA recombination / DNA damage response / magnesium ion binding / ATP hydrolysis activity / DNA binding / ATP binding / cytosol 類似検索 - 分子機能
Biotechnology and Biological Sciences Research Council (BBSRC)
BB/S007261/1
英国
Medical Research Council (MRC, United Kingdom)
英国
引用
ジャーナル: Elife / 年: 2022 タイトル: Structures of RecBCD in complex with phage-encoded inhibitor proteins reveal distinctive strategies for evasion of a bacterial immunity hub. 著者: Martin Wilkinson / Oliver J Wilkinson / Connie Feyerherm / Emma E Fletcher / Dale B Wigley / Mark S Dillingham / 要旨: Following infection of bacterial cells, bacteriophage modulate double-stranded DNA break repair pathways to protect themselves from host immunity systems and prioritise their own recombinases. Here, ...Following infection of bacterial cells, bacteriophage modulate double-stranded DNA break repair pathways to protect themselves from host immunity systems and prioritise their own recombinases. Here, we present biochemical and structural analysis of two phage proteins, gp5.9 and Abc2, which target the DNA break resection complex RecBCD. These exemplify two contrasting mechanisms for control of DNA break repair in which the RecBCD complex is either inhibited or co-opted for the benefit of the invading phage. Gp5.9 completely inhibits RecBCD by preventing it from binding to DNA. The RecBCD-gp5.9 structure shows that gp5.9 acts by substrate mimicry, binding predominantly to the RecB arm domain and competing sterically for the DNA binding site. Gp5.9 adopts a parallel coiled-coil architecture that is unprecedented for a natural DNA mimic protein. In contrast, binding of Abc2 does not substantially affect the biochemical activities of isolated RecBCD. The RecBCD-Abc2 structure shows that Abc2 binds to the Chi-recognition domains of the RecC subunit in a position that might enable it to mediate the loading of phage recombinases onto its single-stranded DNA products.
名称: RecBCD-Abc2-PpiB-DNA complex / タイプ: complex / ID: 1 / 親要素: 0 / 含まれる分子: #1-#5 詳細: All proteins co-expressed and purified as one complex. DNA added prior to making grids in a 1.5x molar excess. Host PpiB interacts with complex and was pulled through purification.
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超分子 #2: RecBCD enzyme subunits RecB, RecC and RecD