Fig. 2: Structural features of SMTA.
From: Biocatalysis enables the scalable conversion of biobased furans into various furfurylamines
a Overall structure of dimeric SMTA. Protomers and bound PLP molecules are represented as a partially transparent cartoon model (pale yellow and cyan) and as a stick model (green), respectively. The N-terminal residues (aa 2–10) involved in the dimeric interaction are presented in purple and orange for each protomer. b The unique interaction of the N-terminal residues (purple and pale cyan) with the residues of the other protomer (yellow) in the SMTA structure. The hydrogen bond is indicated by a dashed line. c The 2fofc omit map (pink, 1.5 σ contour level) is shown on the internal aldimine of PLP that is covalently linked to Lys291 and hydrogen bond-mediating water molecules, which were omitted during the calculation made for map generation. d Superposition of the PLP binding site for SMTA (yellow) and CVTA (gray, PDB entry 4A6T) shows the details of the interaction of the aspartate residue with a salt bridge with the pyridinium nitrogen of PLP. The hydrogen bonds and an ionic interaction are depicted by dashed lines.
