PET hydrolase (PETase), which hydrolyzes polyethylene terephthalate (PET) into soluble building blocks, provides an attractive avenue for the bioconversion of plastics. Here we present the structures of a novel PETase from the PET-consuming microbe Ideonella sakaiensis in complex with substrate and product analogs. Through structural analyses, mutagenesis, and activity measurements, a substrate-binding mode is proposed, and several features critical for catalysis are elucidated.
        
Representative scheme of Polyesterase-lipase-cutinase structure and an image from PDBsum server
no Image
Databases
PDB-Sum
5XH3 Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
5XH3Fold classification based on Structure-Structure alignment of Proteins - FSSP server