Abstract
CRISPRs and Cas proteins form a microbial adaptive immune system against phage infection. To counteract this defense mechanism, phages evolved anti-CRISPR (Acr) proteins that inhibit the CRISPR-Cas systems. Here, we report the crystal structure of AcrIF2, an Acr protein inactivating the type I-F CRISPR-Cas system in Pseudomonas aeruginosa. In the type I-F systems, multiple Cas proteins (Csy1-4) constitute a surveillance complex with a guide RNA for target recognition. We demonstrated that AcrIF2 binds strongly to Csy1-Csy2 subcomplexes from two Xanthomonas species.
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