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Highlights d cryo-EM structure of EcMre11-Rad50 bound to a DNA break d Mre11 dimer binds the DNA end at the side of Rad50 d Mre11 and Rad50 assemble a transient DNA cutting channel d The coiled coils form a rod-shaped DNA gate and clamp

Background: Antifeeding prophage (Afp) is a toxin-delivery bacteriophage tail-like particle. Results: The syringe-like three-dimensional structure, composed of a helical sheath formed by 10 disks, a baseplate, and a central tube displays 6-fold symmetry. Conclusion: Although similar to other type VI secretion systems, Afp possesses unique features. Significance: This is the first insight into the three-dimensional structure of a tailocin.

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