- PDB-7ywa: Structure of DinI in complex with RecA filament -
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基本情報
登録情報
データベース: PDB / ID: 7ywa
タイトル
Structure of DinI in complex with RecA filament
要素
DNA (5'-D(P*TP*TP*TP*TP*TP*T)-3')
DNA damage-inducible protein I
Protein RecA
キーワード
DNA BINDING PROTEIN/DNA / SOS response / Filament / DNA repair / DNA BINDING PROTEIN-DNA COMPLEX
機能・相同性
機能・相同性情報
ATP-dependent DNA damage sensor activity / SOS response / single-stranded DNA binding / DNA recombination / damaged DNA binding / DNA repair / enzyme binding / ATP hydrolysis activity / ATP binding / cytosol 類似検索 - 分子機能
DNA damage-inducible protein DinI-like / DinI-like superfamily / DinI-like family / : / : / RecA C-terminal domain / DNA recombination/repair protein RecA, conserved site / DNA recombination and repair protein RecA, C-terminal / recA signature. / DNA recombination and repair protein RecA ...DNA damage-inducible protein DinI-like / DinI-like superfamily / DinI-like family / : / : / RecA C-terminal domain / DNA recombination/repair protein RecA, conserved site / DNA recombination and repair protein RecA, C-terminal / recA signature. / DNA recombination and repair protein RecA / recA bacterial DNA recombination protein / DNA recombination and repair protein RecA, monomer-monomer interface / RecA family profile 2. / 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
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / DNA / Protein RecA / DNA damage-inducible protein I 類似検索 - 構成要素
National Natural Science Foundation of China (NSFC)
31970040
中国
引用
ジャーナル: Proc Natl Acad Sci U S A / 年: 2023 タイトル: Structural basis for regulation of SOS response in bacteria. 著者: Bo Gao / Liang Liang / Lu Su / Aijia Wen / Chun Zhou / Yu Feng / 要旨: In response to DNA damage, bacterial RecA protein forms filaments with the assistance of DinI protein. The RecA filaments stimulate the autocleavage of LexA, the repressor of more than 50 SOS genes, ...In response to DNA damage, bacterial RecA protein forms filaments with the assistance of DinI protein. The RecA filaments stimulate the autocleavage of LexA, the repressor of more than 50 SOS genes, and activate the SOS response. During the late phase of SOS response, the RecA filaments stimulate the autocleavage of UmuD and λ repressor CI, leading to mutagenic repair and lytic cycle, respectively. Here, we determined the cryo-electron microscopy structures of RecA filaments in complex with DinI, LexA, UmuD, and λCI by helical reconstruction. The structures reveal that LexA and UmuD dimers bind in the filament groove and cleave in an intramolecular and an intermolecular manner, respectively, while λCI binds deeply in the filament groove as a monomer. Despite their distinct folds and oligomeric states, all RecA filament binders recognize the same conserved protein features in the filament groove. The SOS response in bacteria can lead to mutagenesis and antimicrobial resistance, and our study paves the way for rational drug design targeting the bacterial SOS response.