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Journal Article

Crystal structure of the plasmid maintenance system ε /ζ : Functional mechanism of toxin ζ and inactivation by ε 2ζ 2 complex formation

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Meinhart, Anton
mRNA Processing, Max Planck Institute for Medical Research, Max Planck Society;
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Meinhart, A., Alonso, J. C., Sträter, N., & Saenger, W. (2003). Crystal structure of the plasmid maintenance system ε /ζ: Functional mechanism of toxin ζ and inactivation by ε 2ζ 2 complex formation. Proceedings of the National Academy of Sciences of the USA, 100(4), 1661-1666. doi:10.1073/pnas.0434325100.

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 varε /ζ and antibiotic resistance proteins, among others. The crystal structure of the biologically nontoxic varε 2ζ 2 protein complex at a 1.95−Å resolution and site−directed mutagenesis showed that free ζacts as phosphotransferase by using ATP/GTP. In varepsilon 2ζ 2, the toxin zeta is inactivated because the N−terminal helix of the antitoxin varepsilon blocks the ATP/GTP−binding site. To our knowledge, this is the first prokaryotic postsegregational killing system that has been entirely structurally characterized