3HL8

Crystal structure of exonuclease I in complex with inhibitor BCBP

3HL8 の概要

• エントリーDOI: 10.2210/pdb3hl8/pdb
• 関連するPDBエントリー: 3C94 3C95 3HP9
• 分子名称: Exodeoxyribonuclease I, MAGNESIUM ION, (5R)-3-tert-butyl-1-(6-chloro-1,3-benzothiazol-2-yl)-4,5-dihydro-1H-pyrazol-5-ol, ... (6 entities in total)
• 機能のキーワード: exonuclease, ssb, genome maintenance, dna damage, dna repair, hydrolase, nuclease
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56185.14

構造登録者

Satyshur, K.A. (登録日: 2009-05-27, 公開日: 2010-01-19, 最終更新日: 2025-12-03)

主引用文献

Lu, D.,Bernstein, D.A.,Satyshur, K.A.,Keck, J.L.
Small-molecule tools for dissecting the roles of SSB/protein interactions in genome maintenance
Proc.Natl.Acad.Sci.USA, 107:633-638, 2010

PubMed Abstract: Bacterial single-stranded DNA-binding proteins (SSBs) help to recruit a diverse array of genome maintenance enzymes to their sites of action through direct protein interactions. For all cases examined to date, these interactions are mediated by the evolutionarily conserved C terminus of SSB (SSB-Ct). The essential nature of SSB protein interactions makes inhibitors that block SSB complex formation valuable biochemical tools and attractive potential antibacterial agents. Here, we identify four small molecules that disrupt complexes formed between Escherichia coli SSB and Exonuclease I (ExoI), a well-studied SSB-interacting enzyme. Each compound disrupts ExoI/SSB-Ct peptide complexes and abrogates SSB stimulation of ExoI nuclease activity. Structural and biochemical studies support a model for three of the compounds in which they compete with SSB for binding to ExoI. The fourth appears to rely on an allosteric mechanism to disrupt ExoI/SSB complexes. Subsets of the inhibitors block SSB-Ct complex formation with two other SSB-interaction partners as well, which highlights their utility as reagents for investigating the roles of SSB/protein interactions in diverse DNA replication, recombination, and repair reactions.

PubMed: 20018747
DOI: 10.1073/pnas.0909191107

実験手法

X-RAY DIFFRACTION (1.55 Å)