Functional plasticity of antibacterial EndoU toxins

What is it about?

EndoU ribonucleases are commonly used as weapons in inter-bacterial conflict. We present the first structure of a bacterial EndoU toxin domain. The CdiA-CTSTECO31 toxin shares the same fold and catalytic triad as RNA processing enzymes from Xenopus laevis and human SARS virus. Unlike the eukaryotic EndoU ribonucleases, CdiA-CTSTECO31 is exquisitely specific for the anticodon loop of tRNAGlu. These findings suggest that the EndoU fold is a versatile scaffold for the evolution of novel substrate specificities.

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