Fig. 3: The structure of SuCphA1 N domain with bound cyanophycin.
From: A cryptic third active site in cyanophycin synthetase creates primers for polymerization
a Structure of SuCphA1 in complex with cyanophycin substrate in both the G domain active site (sticks) and N domain active site (spheres). b The SuCphA1 N domain in complex with (β-Asp-Arg)16 as a substrate. Seven dipeptide residues are visible. Polymer binding residues and their interactions are highlighted. P4, P3, P2, P1, P1’, P2’, P3’ denote β-Asp-Arg dipeptides numbered relative to the cleavage point. c Close-up view of the structure of SuCphA1 in complex with cyanophycin substrate. d The structure of SuCphA1 in complex with in situ cleaved cyanophycin. Four dipeptide residues are visible. Polymer binding residues and their interactions are highlighted.
