8GMT

Structure of UmuD in complex with RecA filament

8GMT の概要

• エントリーDOI: 10.2210/pdb8gmt/pdb
• EMDBエントリー: 34153
• 分子名称: DNA polymerase V subunit UmuD, DNA (5'-D(P*TP*TP*TP*TP*TP*T)-3'), Protein RecA, ... (5 entities in total)
• 機能のキーワード: sos response, reca, umud, filament, dna repair, helical reconstruction, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 108942.27

構造登録者

Gao, B.,Feng, Y. (登録日: 2022-08-22, 公開日: 2022-12-21, 最終更新日: 2024-07-03)

主引用文献

Gao, B.,Liang, L.,Su, L.,Wen, A.,Zhou, C.,Feng, Y.
Structural basis for regulation of SOS response in bacteria.
Proc.Natl.Acad.Sci.USA, 120:e2217493120-e2217493120, 2023

PubMed Abstract: 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.

PubMed: 36598938
DOI: 10.1073/pnas.2217493120

実験手法

ELECTRON MICROSCOPY (3.31 Å)