Figure 1: The structure of AcrF1 allowed the identification of a functional interface. | Nature Communications

Figure 1: The structure of AcrF1 allowed the identification of a functional interface.

From: The solution structure of an anti-CRISPR protein

Figure 1

(a) The NMR solution structure of AcrF1. Overlay of 20 lowest energy AcrF1 structures showing the best-fit superposition of the backbone atoms (N, Cα and C′). (b) Ribbon representation of AcrF1 showing the positions of the three residues that are critical for AcrF1 function in vivo. (c) Tenfold serial dilutions of phage lysates with a starting concentration of 107 pfu mL−1 were spotted onto a lawn of bacteria containing an active type I-F CRISPR–Cas system. Replication of CRISPR-sensitive phage DMS3m is inhibited unless a fully functional AcrF1 anti-CRISPR is expressed from a plasmid within the cells. Phage DMS3 is not targeted by the CRISPR–Cas system. Phage replication results in round zones of clearing of the bacterial lawn. Y14A is a fully active mutant shown for comparison.

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