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Reveals GTP hydrolysis's role in DNA cleavage through phosphorothioate recognition, suggesting new avenues for phage resistance.
3234/A. We elucidate its conserved "recognize-hydrolyze-activate" mechanism: the effector EcSspE integrates PT recognition, GTP hydrolysis, and allosteric signaling to license DNA cleavage. Beyond this paradigm, we reveal that subtle evolutionary refinements in its quaternary architecture-a streamlined, side-by-side assembly with a reduced interface-amplify defensive output by enhancing conformational dynamics. This insight bridges structural biophysics and immunity. The system's strict PT-dependence ensures biosafety, and its defined mechanistic logic and key molecular switches (Y63, R133, N724) establish a framework for engineering programmable phage resistance, advancing both our understanding of host-virus conflict and our ability to harness it.
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Yufeng et al. (2026) studied this question.
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