Fig. 2
From: Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate
Structure of I. sakaiensis MHETase bound to a nonhydrolyzable MHET analog. The structure explains substrate specificity and reveals an induced-fit substrate-binding mode. a Co-structure of MHETase bound to MHETA (yellow), α/β-hydrolase domain (MHETaseHyd) in orange, lid domain (MHETaseLid) in marine blue. Inset, bottom left—refined FO−FC-omit electron density map (green) contoured at 3σ for MHETA. MHETA of the refined final structure is shown as sticks. b Close-up view on MHETA (yellow) bound to the active site of MHETase. c, d Molecular surface of the MHETase active site c without and d with bound MHETA, the catalytic triad and F415 are shown as sticks. e Close-up view of the tannin acyl α/β-hydrolase active site from L. plantarum (PDB-ID: 4J0K25) bound to ethyl gallate (EthGal, yellow), superimposed on helix α5 of MHETase (not shown). α/β-Hydrolase domain (LptEHyd) in olive, lid domain (LptELid) in dark blue. Rotation symbols indicate views relative to a. Color scheme for interacting residues and water oxygens as in Fig. 1. Calcium is shown as magenta spheres
