Extended Data Fig. 6: Detailed interactions between activated Ba1Cas12a3 and tRNAAla(UGC).
From: RNA-triggered Cas12a3 cleaves tRNA tails to execute bacterial immunity
(a) Interactions between the REC2 loop of Ba1Cas12a3 and the T-arm of tRNA are shown with underlying EM density map. (b) Interactions between the tRLD of Ba1Cas12a3 and the 3′ CCA tail of the tRNA with underlying EM density map. (c) 2D interaction plot displaying the binding interface between Ba1Cas12a3 and tRNA. Electrostatic contacts are primarily between positively charged side chains or peptide backbone amines located at the ends of helices. Several residues (e.g., N253 and K1038) make contacts within the minor groove of RNA-duplexes, likely sensing the specific shape of the tRNA. (d) The bound tRNA is modeled with a tryptophan residue, demonstrating no steric clashes in the structure to impair binding to aminoacylated tRNAs.
