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

Meinhart, Anton; Alonso, Juan C.; Sträter, Norbert; Saenger, Wolfram

doi:10.1073/pnas.0434325100

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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 United States of America, 100(4), 1661-1666. doi:10.1073/pnas.0434325100.

Cite as: https://hdl.handle.net/21.11116/0000-0000-3D6A-6

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 ɛ/ζ and antibiotic resistance proteins, among others. The crystal structure of the biologically nontoxic ɛ2ζ2 protein complex at a 1.95-Å resolution and site-directed mutagenesis showed that free ζ acts as phosphotransferase by using ATP/GTP. In ɛ2ζ2, the toxin ζ is inactivated because the N-terminal helix of the antitoxin ɛ blocks the ATP/GTP-binding site. To our knowledge, this is the first prokaryotic postsegregational killing system that has been entirely structurally characterized.