5XG0

Crystal structure of a novel PET hydrolase from Ideonella sakaiensis 201-F6

Summary for 5XG0

Entry DOI	10.2210/pdb5xg0/pdb
Related	5XFX 5XFY 5XFZ
Descriptor	Poly(ethylene terephthalate) hydrolase (2 entities in total)
Functional Keywords	metal-binding, substrate binding, acidocalcisomal pyrophosphatase, inhibitor, hydrolase
Biological source	Ideonella sakaiensis (strain 201-F6)
Total number of polymer chains	3
Total formula weight	83600.79
Authors	Han, X.,Liu, W.D.,Zheng, Y.Y.,Chen, C.C.,Guo, R.T. (deposition date: 2017-04-11, release date: 2017-12-20, Last modification date: 2023-11-22)
Primary citation	Han, X.,Liu, W.,Huang, J.W.,Ma, J.,Zheng, Y.,Ko, T.P.,Xu, L.,Cheng, Y.S.,Chen, C.C.,Guo, R.T. Structural insight into catalytic mechanism of PET hydrolase Nat Commun, 8:2106-2106, 2017 Cited by PubMed Abstract: 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. PubMed: 29235460 DOI: 10.1038/s41467-017-02255-z PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.58 Å)

Structure validation