3TND

Crystal structure of Shigella flexneri VapBC toxin-antitoxin complex

3TND の概要

• エントリーDOI: 10.2210/pdb3tnd/pdb
• 分子名称: tRNA(fMet)-specific endonuclease VapC, Antitoxin VapB, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: pin domain, spovt/abrb-like domain, ribonuclease, dna-binding, translation, toxin
• 由来する生物種: Shigella flexneri; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 98064.88

構造登録者

Dienemann, C.,Boggild, A.,Winther, K.S.,Gerdes, K.,Brodersen, D.E. (登録日: 2011-09-01, 公開日: 2011-11-02, 最終更新日: 2024-02-28)

主引用文献

Dienemann, C.,Boggild, A.,Winther, K.S.,Gerdes, K.,Brodersen, D.E.
Crystal Structure of the VapBC Toxin-Antitoxin Complex from Shigella flexneri Reveals a Hetero-Octameric DNA-Binding Assembly.
J.Mol.Biol., 414:713-722, 2011

PubMed Abstract: Toxin-antitoxin (TA) loci are common in archaea and prokaryotes and allow cells to rapidly adapt to changing environmental conditions through release of active regulators of metabolism. Many toxins are endonucleases that target cellular mRNA and tRNAs, while the antitoxins tightly wrap around the toxins to inhibit them under normal circumstances. The antitoxins also bind to operators in the promoter regions of the cognate TA operon and thereby regulate transcription. For enteric vapBC TA loci, the VapC toxins specifically cleave tRNA(fMet) and thus down-regulate protein synthesis. Here, we describe the crystal structure of the intact Shigella flexneri VapBC TA complex, determined to 2.7 Å resolution. Both in solution and in the crystal structure, four molecules of each protein combine to form a large and globular hetero-octameric assembly with SpoVT/AbrB-type DNA-binding domains at each end and a total molecular mass of about 100 kDa. The structure gives new insights into the inhibition of VapC toxins by VapB and provides the molecular basis for understanding transcriptional regulation through VapB dimerization.

PubMed: 22037005
DOI: 10.1016/j.jmb.2011.10.024

実験手法

X-RAY DIFFRACTION (2.7 Å)