Extended Data Fig. 5: Structural comparison of the quaternary structures of SuCas12a2 and Ba1Cas12a3.
From: RNA-triggered Cas12a3 cleaves tRNA tails to execute bacterial immunity
(a) Model of the SuCas12a2-crRNA-target RNA-dsDNA quaternary complex. (b) Model of the Ba1Cas12a3-crRNA-target RNA-tRNAAla(UGC) quaternary complex. (c) The interaction between the PI domain and the PFS nucleotides in the SuCas12a2 quaternary complex. The bases of the PFS at position +2 (A22-Q681), +3 (A23-K621, A23-N625), and +4 (A24-I633) interact with the SuCas12a2 PI domain. (d) The interaction between the PI domain and the PFS nucleotides in the Ba1Cas12a3 quaternary complex. The base of adenine at position +2 (A37-S469) interacts with the Ba1Cas12a3 PI domain. (e) Ba1Cas12a3 PI domain (in plum) superimposed with SuCas12a2 PI domain (in dark grey). The PFS for Ba1Cas12a3 is colored in dark orange. The PFS for SuCas12a2 is colored in dim grey. The PFS sequences bind to each PI domain in a distinct manner. The differences between SuCas12a2 and Ba1Cas12a3 in PFS recognition pattern are well correlated with the PFS library screening in Supplementary Fig. 2a.
