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Table 1 Anti-CRISPR proteins and their mechanisms of action

From: Structural insights into the inactivation of CRISPR-Cas systems by diverse anti-CRISPR proteins

Anti-CRISPR (source) Size (amino acids) CRISPR inhibited Inhibition mechanism Structure (PDB code) Citation
AcrE1 (P. aeruginosa) 100 Type I-E [31]
AcrE2 (P. aeruginosa) 84 Type I-E [31]
AcrE3 (P. aeruginosa) 68 Type I-E [31]
AcrE4 (P. aeruginosa) 52 Type I-E [31]
AcrF1 (P. aeruginosa) 78 Type I-F Inhibits DNA binding 2LW5,5UZ9,6ANV,6B46 [30, 36,37,38,39]
AcrF2 (P. aeruginosa) 90 Type I-F Partially overlaps with the binding site of dsDNA 5UZ9,6B47 [30, 36, 39]
AcrF3 (P. aeruginosa) 139 Type I-F Blocks the entrance of the DNA binding tunnel; blocks new sequence acquisition 5GNF,5GQH,5B7I [30, 40,41,42]
AcrF4 (P. aeruginosa) 100 Type I-F [30]
AcrF5 (P. aeruginosa) 79 Type I-F [30]
AcrF6 (P. aeruginosa) 100 Type I-E/F [32]
AcrF7 (P. aeruginosa) 67 Type I-F [32]
AcrF8 (P. atrosepticum) 92 Type I-F [32]
AcrF9 (V. parahaemolyticus) 68 Type I-F [32]
AcrF10 (S. xiamenensis) 97 Type I-F DNA mimic, blocks DNA binding 6ANW,6B48 [32, 39]
AcrIIA1 (L. monocytogenes) 149 Type II-A 5Y6A [51, 60]
AcrIIA2 (L. monocytogenes) 123 Type II-A Inhibits DNA binding [51]
AcrIIA3 (L. monocytogenes) 125 Type II-A [51]
AcrIIA4 (L. monocytogenes) 87 Type II-A PAM mimic, inhibits DNA binding; interacts with active site within the RuvC domain; hinders the conformation change of the HNH domain 5XBL,5VW1,5VZL [51, 55,56,57]
AcrIIA5 (S. thermophilus) 140 Type II-A [54]
AcrIIC1 (N. meningitidis) 85 Type II-C Binds the HNH domain; shields the catalytic center 5VGB [50, 59]
AcrIIC2 (N. meningitidis) 123 Type II-C [50]
AcrIIC3 (N. meningitidis) 116 Type II-C Induces Cas9 dimerization; inhibits DNA binding [50, 59]