5YFE

Enzymatic and structural characterization of the poly (ethylene terephthalate) hydrolase PETase from I. sakaiensis

Summary for 5YFE

• Entry DOI: 10.2210/pdb5yfe/pdb
• Descriptor: Poly(ethylene terephthalate) hydrolase, SULFATE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: pet degradation, hydrolase
• Biological source: Ideonella sakaiensis (strain 201-F6)
• Total number of polymer chains: 1
• Total formula weight: 29069.02

Authors

Bao, R.,He, L.H.,Liu, B. (deposition date: 2017-09-21, release date: 2018-09-26, Last modification date: 2024-10-16)

Primary citation

Liu, B.,He, L.,Wang, L.,Li, T.,Li, C.,Liu, H.,Luo, Y.,Bao, R.
Protein Crystallography and Site-Direct Mutagenesis Analysis of the Poly(ethylene terephthalate) Hydrolase PETase from Ideonella sakaiensis.
Chembiochem, 2018

PubMed Abstract: Unlike traditional recycling strategies, biodegradation is a sustainable solution for disposing of poly(ethylene terephthalate) (PET) waste. PETase, a newly identified enzyme from Ideonella sakaiensis, has high efficiency and specificity towards PET and is, thus, a prominent candidate for PET degradation. On the basis of biochemical analysis, we propose that a wide substrate-binding pocket is critical for its excellent ability to hydrolyze crystallized PET. Structure-guided site-directed mutagenesis revealed an improvement in PETase catalytic efficiency, providing valuable insight into how the molecular engineering of PETase can optimize its application in biocatalysis.

PubMed: 29603535
DOI: 10.1002/cbic.201800097

Experimental method

X-RAY DIFFRACTION (1.39 Å)