6ILW

Crystal structure of PETase from Ideonella sakaiensis

Summary for 6ILW

• Entry DOI: 10.2210/pdb6ilw/pdb
• Descriptor: Poly(ethylene terephthalate) hydrolase, CHLORIDE ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: crystal strcuture of petase from ideonella sakaiensis, hydrolase
• Biological source: Ideonella sakaiensis (strain 201-F6)
• Total number of polymer chains: 1
• Total formula weight: 28599.09

Authors

Liu, C.C.,Shi, C. (deposition date: 2018-10-19, release date: 2019-03-27, Last modification date: 2024-10-23)

Primary citation

Liu, C.,Shi, C.,Zhu, S.,Wei, R.,Yin, C.C.
Structural and functional characterization of polyethylene terephthalate hydrolase from Ideonella sakaiensis.
Biochem. Biophys. Res. Commun., 508:289-294, 2019

PubMed Abstract: Polyethylene terephthalate (PET) hydrolase from Ideonella sakaiensis (IsPETase) can be used to degrade PET. In order to use IsPETase in industry, we studied the enzymatic activity of IsPETase in different conditions containing environmental and physicochemical factors commonly found in nature. We observed that salts and glycerol enhanced the enzymatic activity, while detergents and organic solvents reduced the enzymatic activity. IsPETase hydrolyzed p-nitrophenyl (p-NP) esters instead of naphthyl esters. To make IsPETase an enzyme capable of hydrolyzing naphthyl esters, site-directed mutagenesis was carried out based on the structural information provided by the crystal structure. We found that the IsPETase, IsPETase, and IsPETase mutants can hydrolyze naphthyl esters. IsPETase engineering can direct researchers to use this α/β-hydrolase protein scaffold to design enzymes that can hydrolyze a variety of polyesters.

PubMed: 30502092
DOI: 10.1016/j.bbrc.2018.11.148

Experimental method

X-RAY DIFFRACTION (1.575 Å)