Fig. 2: Structural analysis of GsSir2 and pAgo.
From: Structural basis of antiphage immunity generated by a prokaryotic Argonaute-associated SPARSA system
a The structure of GsSir2 is composed of an N-terminal Sir2 and C-terminal APAZ ___domain, i.e., the N-terminal Sir2 ___domain (residues 1–309, colored cyan) and the C-terminal APAZ (residues 331–587, colored green). The linker (residues 309–331) interconnecting the two domains is shown as a gray line. b Sequence alignment of Sir2 and its homologs. The conserved putative catalytic residues are indicated using a circular ring in cyan. c NAD+ assumption of wild-type SPARSA and the mutants on N142 and H186 SPARSA. Each value is the mean ± SD and from more than three replicates. d Superimposition of the GsSir2 N-terminal ___domain and the Sir2 ___domain of ThsA. e The close-up view of the overlay shows the difference in the Sir2 ___domain, and the catalytic residues N142 and H186 of Sir2--APAZ are highlighted in the sticks. f Superimposition of the APAZ ___domain the N ___domain, and PAZ ___domain of human hAgo2 (PDB 4F3T). g The structure of pAgo. h The structure of AfAgo (PDB: 1YTU). i Superimposition of pAgo with AfAgo.
