7U02

Structure of the C. crescentus DriD C-domain bound to ssDNA

7U02 の概要

• エントリーDOI: 10.2210/pdb7u02/pdb
• 分子名称: WYL domain-containing protein, DNA (5'-D(P*AP*CP*G)-3'), SULFATE ION, ... (4 entities in total)
• 機能のキーワード: drid, dna repair, sos-independent repair, dida, transcription
• 由来する生物種: Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 44676.26

構造登録者

Schumacher, M.A. (登録日: 2022-02-17, 公開日: 2022-06-01, 最終更新日: 2024-02-21)

主引用文献

Gozzi, K.,Salinas, R.,Nguyen, V.D.,Laub, M.T.,Schumacher, M.A.
ssDNA is an allosteric regulator of the C. crescentus SOS-independent DNA damage response transcription activator, DriD.
Genes Dev., 36:618-633, 2022

PubMed Abstract: DNA damage repair systems are critical for genomic integrity. However, they must be coordinated with DNA replication and cell division to ensure accurate genomic transmission. In most bacteria, this coordination is mediated by the SOS response through LexA, which triggers a halt in cell division until repair is completed. Recently, an SOS-independent damage response system was revealed in This pathway is controlled by the transcription activator, DriD, but how DriD senses and signals DNA damage is unknown. To address this question, we performed biochemical, cellular, and structural studies. We show that DriD binds a specific promoter DNA site via its N-terminal HTH domain to activate transcription of genes, including the cell division inhibitor A structure of the C-terminal portion of DriD revealed a WYL motif domain linked to a WCX dimerization domain. Strikingly, we found that DriD binds ssDNA between the WYL and WCX domains. Comparison of apo and ssDNA-bound DriD structures reveals that ssDNA binding orders and orients the DriD domains, indicating a mechanism for ssDNA-mediated operator DNA binding activation. Biochemical and in vivo studies support the structural model. Our data thus reveal the molecular mechanism underpinning an SOS-independent DNA damage repair pathway.

PubMed: 35618312
DOI: 10.1101/gad.349541.122

実験手法

X-RAY DIFFRACTION (2.48 Å)