3DD7

Structure of DocH66Y in complex with the C-terminal domain of Phd

3DD7 の概要

• エントリーDOI: 10.2210/pdb3dd7/pdb
• 関連するPDBエントリー: 3DD9
• 分子名称: Death on curing protein, Prevent host death protein, BROMIDE ION, ... (4 entities in total)
• 機能のキーワード: all alpha, ribosome inhibitor
• 由来する生物種: Enterobacteria phage P1; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 36116.95

構造登録者

Garcia-Pino, A.,Loris, R. (登録日: 2008-06-05, 公開日: 2008-09-16, 最終更新日: 2024-11-06)

主引用文献

Garcia-Pino, A.,Christensen-Dalsgaard, M.,Wyns, L.,Yarmolinsky, M.,Magnuson, R.D.,Gerdes, K.,Loris, R.
Doc of Prophage P1 Is Inhibited by Its Antitoxin Partner Phd through Fold Complementation
J.Biol.Chem., 283:30821-30827, 2008

PubMed Abstract: Prokaryotic toxin-antitoxin modules are involved in major physiological events set in motion under stress conditions. The toxin Doc (death on curing) from the phd/doc module on phage P1 hosts the C-terminal domain of its antitoxin partner Phd (prevents host death) through fold complementation. This Phd domain is intrinsically disordered in solution and folds into an alpha-helix upon binding to Doc. The details of the interactions reveal the molecular basis for the inhibitory action of the antitoxin. The complex resembles the Fic (filamentation induced by cAMP) proteins and suggests a possible evolutionary origin for the phd/doc operon. Doc induces growth arrest of Escherichia coli cells in a reversible manner, by targeting the protein synthesis machinery. Moreover, Doc activates the endogenous E. coli RelE mRNA interferase but does not require this or any other known chromosomal toxin-antitoxin locus for its action in vivo.

PubMed: 18757857
DOI: 10.1074/jbc.M805654200

実験手法

X-RAY DIFFRACTION (1.7 Å)