3HS2

Crystal structure of PHD truncated to residue 57 in an orthorhombic space group

3HS2 の概要

• エントリーDOI: 10.2210/pdb3hs2/pdb
• 関連するPDBエントリー: 3DD7 3HRY
• 分子名称: Prevent host death protein, SULFATE ION (3 entities in total)
• 機能のキーワード: prevent host death, phd, intrinsic disorder, doc, toxin-antitoxin, antitoxin
• 由来する生物種: Enterobacteria phage P1 (Bacteriophage P1)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 51729.52

構造登録者

Garcia-Pino, A.,Loris, R. (登録日: 2009-06-10, 公開日: 2010-06-23, 最終更新日: 2023-09-06)

主引用文献

Garcia-Pino, A.,Balasubramanian, S.,Wyns, L.,Gazit, E.,De Greve, H.,Magnuson, R.D.,Charlier, D.,van Nuland, N.A.,Loris, R.
Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity.
Cell(Cambridge,Mass.), 142:101-111, 2010

PubMed Abstract: Regulation of the phd/doc toxin-antitoxin operon involves the toxin Doc as co- or derepressor depending on the ratio between Phd and Doc, a phenomenon known as conditional cooperativity. The mechanism underlying this observed behavior is not understood. Here we show that monomeric Doc engages two Phd dimers on two unrelated binding sites. The binding of Doc to the intrinsically disordered C-terminal domain of Phd structures its N-terminal DNA-binding domain, illustrating allosteric coupling between highly disordered and highly unstable domains. This allosteric effect also couples Doc neutralization to the conditional regulation of transcription. In this way, higher levels of Doc tighten repression up to a point where the accumulation of toxin triggers the production of Phd to counteract its action. Our experiments provide the basis for understanding the mechanism of conditional cooperative regulation of transcription typical of toxin-antitoxin modules. This model may be applicable for the regulation of other biological systems.

PubMed: 20603017
DOI: 10.1016/j.cell.2010.05.039

実験手法

X-RAY DIFFRACTION (2.2 Å)