Cover: Colicin E5, as a bacterial toxin, specifically cleaves the G-U sequences in the anticodons of tRNAs for Asp, Asn, His, and Tyr. Crystal structures of the C-terminal tRNase domain of colicin E5 (E5-CRD; yellow) and its cognate inhibitor protein (pink) complex (right), and the complex of E5-CRD with its substrate analogue revealed how E5 recognizes the targets specifically. The binding modes of both complexes mimic the Watson–Crick type mRNA–tRNA interactions. The docking model of E5-CRD with a tRNA (left) also suggested its preference of tRNAs to free RNAs. See Yajima et al. (2006), Nucleic Acids Res., 34, 6074–6082.
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