Extended Data Fig. 3: Comparison of CphA1 active sites to homologous enzymes.
From: Structures and function of the amino acid polymerase cyanophycin synthetase
a, Overlay of SuCphA1 G domain and bifunctional glutathione synthetase from S. agalactiae (PDB code 3LN6) showing the similar ATP binding mode and conserved residues. b, Overlay of SuCphA1 G domain and glutathione synthetase from E. coli (PDB code 1GSA) showing the similar substrate orientation and overall structure. c, Overlay of SuCphA1 M domain and MurE ligase from M. tuberculosis residues (PDB code 2WTZ) showing the similar ATP binding mode and conserved, and (d) similar substrate orientation. e, The interactions made by cyanophycin with residues in the M domain of SuCphA1. f, The three versions of cyanophycin and cyanophycin analogs used for the determined structures of SuCphA1 presented in this study.
