Fig. 4: Homology model of AcrIIA6123.
From: A truncated anti-CRISPR protein prevents spacer acquisition but not interference
A Sequence alignment of AcrIIA6123 and AcrIIA6D1811 (residues 59–183). Secondary structure elements from the crystal structure of AcrIIA6D1811 are shown above the alignment. B Ribbon representation of the AcrIIA6123 homology model (left, colors representing secondary structure elements) superimposed on the crystal structure of AcrIIA6D1811 (right, pale yellow). C Representation of sequence variations between AcrIIA6123 and AcrIIA6D1811. Gray areas represent 100% sequence identity. Red patches represent amino acid substitutions. D Surface representations of AcrIIA6123 (left) and AcrIIA6D1811 (right) dimeric assemblies. The dotted arrow indicates the dimerization interface missing in the AcrIIA6123 dimer. E Comparison between the simulated binding interface of AcrIIA6123 to St1Cas9-RNA complex (left) and the experimentally demonstrated binding of AcrIIA6D1811 to St1Cas9-RNA complex (right).
