4G6U

CdiA-CT/CdiI toxin and immunity complex from Escherichia coli

4G6U の概要

• エントリーDOI: 10.2210/pdb4g6u/pdb
• 関連するPDBエントリー: 4G6V
• 分子名称: EC869 CdiA-CT, EC869 CdiI, ZINC ION, ... (7 entities in total)
• 機能のキーワード: beta-augmentation, dnase, toxin, immunity
• 由来する生物種: Escherichia coli O157:H7; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53668.37

構造登録者

Morse, R.P.,Nikolakakis, K.,Willet, J.,Gerrick, E.,Low, D.A.,Hayes, C.S.,Goulding, C.W. (登録日: 2012-07-19, 公開日: 2012-12-12, 最終更新日: 2024-10-16)

主引用文献

Morse, R.P.,Nikolakakis, K.C.,Willett, J.L.,Gerrick, E.,Low, D.A.,Hayes, C.S.,Goulding, C.W.
Structural basis of toxicity and immunity in contact-dependent growth inhibition (CDI) systems.
Proc.Natl.Acad.Sci.USA, 109:21480-21485, 2012

PubMed Abstract: Contact-dependent growth inhibition (CDI) systems encode polymorphic toxin/immunity proteins that mediate competition between neighboring bacterial cells. We present crystal structures of CDI toxin/immunity complexes from Escherichia coli EC869 and Burkholderia pseudomallei 1026b. Despite sharing little sequence identity, the toxin domains are structurally similar and have homology to endonucleases. The EC869 toxin is a Zn(2+)-dependent DNase capable of completely degrading the genomes of target cells, whereas the Bp1026b toxin cleaves the aminoacyl acceptor stems of tRNA molecules. Each immunity protein binds and inactivates its cognate toxin in a unique manner. The EC869 toxin/immunity complex is stabilized through an unusual β-augmentation interaction. In contrast, the Bp1026b immunity protein exploits shape and charge complementarity to occlude the toxin active site. These structures represent the initial glimpse into the CDI toxin/immunity network, illustrating how sequence-diverse toxins adopt convergent folds yet retain distinct binding interactions with cognate immunity proteins. Moreover, we present visual demonstration of CDI toxin delivery into a target cell.

PubMed: 23236156
DOI: 10.1073/pnas.1216238110

実験手法

X-RAY DIFFRACTION (2.353 Å)