1GVN

Crystal Structure of the Plasmid Maintenance System epsilon/zeta: Meachnism of toxin inactivation and toxin function

1GVN の概要

• エントリーDOI: 10.2210/pdb1gvn/pdb
• 分子名称: EPSILON, ZETA, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: postsegregational killing system, plasmid
• 由来する生物種: STREPTOCOCCUS PYOGENES; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 86550.50

構造登録者

Meinhart, A.,Alonso, J.C.,Straeter, N.,Saenger, W. (登録日: 2002-02-19, 公開日: 2003-01-29, 最終更新日: 2024-05-08)

主引用文献

Meinhart, A.,Alonso, J.C.,Strater, N.,Saenger, W.
Crystal Structure of the Plasmid Maintenance System Epsilon /Zeta : Functional Mechanism of Toxin Zeta and Inactivation by Epsilon 2 Zeta 2 Complex Formation
Proc.Natl.Acad.Sci.USA, 100:1661-, 2003

PubMed Abstract: Programmed cell death in prokaryotes is frequently found as postsegregational killing. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid. The broad-host-range, low-copy-number plasmid pSM19035 from Streptococcus pyogenes carries the genes encoding the antitoxin/toxin system epsilon/zeta and antibiotic resistance proteins, among others. The crystal structure of the biologically nontoxic epsilon(2)zeta(2) protein complex at a 1.95-A resolution and site-directed mutagenesis showed that free zeta acts as phosphotransferase by using ATPGTP. In epsilon(2)zeta(2), the toxin zeta is inactivated because the N-terminal helix of the antitoxin epsilon blocks the ATPGTP-binding site. To our knowledge, this is the first prokaryotic postsegregational killing system that has been entirely structurally characterized.

PubMed: 12571357
DOI: 10.1073/PNAS.0434325100

実験手法

X-RAY DIFFRACTION (1.95 Å)