3GA8

Structure of the N-terminal domain of the E. coli protein MqsA (YgiT/b3021)

3GA8 の概要

• エントリーDOI: 10.2210/pdb3ga8/pdb
• 関連するPDBエントリー: 3FMY 3GN5 3HI2
• 分子名称: HTH-type transcriptional regulator MqsA (YgiT/B3021), ZINC ION, 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL, ... (4 entities in total)
• 機能のキーワード: helix-turn-helix, zn-binding protein, dna-binding, transcription, transcription regulation, dna binding protein
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9134.02

構造登録者

Brown, B.L.,Arruda, J.M.,Peti, W.,Page, R. (登録日: 2009-02-16, 公開日: 2010-01-12, 最終更新日: 2024-02-21)

主引用文献

Brown, B.L.,Grigoriu, S.,Kim, Y.,Arruda, J.M.,Davenport, A.,Wood, T.K.,Peti, W.,Page, R.
Three dimensional structure of the MqsR:MqsA complex: a novel TA pair comprised of a toxin homologous to RelE and an antitoxin with unique properties.
Plos Pathog., 5:e1000706-e1000706, 2009

PubMed Abstract: One mechanism by which bacteria survive environmental stress is through the formation of bacterial persisters, a sub-population of genetically identical quiescent cells that exhibit multidrug tolerance and are highly enriched in bacterial toxins. Recently, the Escherichia coli gene mqsR (b3022) was identified as the gene most highly upregulated in persisters. Here, we report multiple individual and complex three-dimensional structures of MqsR and its antitoxin MqsA (B3021), which reveal that MqsR:MqsA form a novel toxin:antitoxin (TA) pair. MqsR adopts an alpha/beta fold that is homologous with the RelE/YoeB family of bacterial ribonuclease toxins. MqsA is an elongated dimer that neutralizes MqsR toxicity. As expected for a TA pair, MqsA binds its own promoter. Unexpectedly, it also binds the promoters of genes important for E. coli physiology (e.g., mcbR, spy). Unlike canonical antitoxins, MqsA is also structured throughout its entire sequence, binds zinc and coordinates DNA via its C- and not N-terminal domain. These studies reveal that TA systems, especially the antitoxins, are significantly more diverse than previously recognized and provide new insights into the role of toxins in maintaining the persister state.

PubMed: 20041169
DOI: 10.1371/journal.ppat.1000706

実験手法

X-RAY DIFFRACTION (1.7 Å)