Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation
By S. Joo, Injin Cho, Hogyun Seo, H. Son, Hye-Young Sagong, T. Shin, S. Choi, Sang Yup Lee, Kyung-Jin Kim. Nature Communications, 2018
622 citations recorded by the source corpus.
Plastics, including poly(ethylene terephthalate) (PET), possess many desirable characteristics and thus are widely used in daily life. However, non-biodegradability, once thought to be an advantage offered by plastics, is causing major environmental problem. Recently, a PET-degrading bacterium, Ideonella sakaiensis, was identified and suggested for possible use in degradation and/or recycling of PET. However, the molecular mechanism of PET degradation is not known. Here we report the crystal structure of I. sakaiensis PETase (IsPETase) at 1.5 Å resolution. IsPETase has a Ser–His-Asp catalytic triad at its active site and contains an optimal substrate binding site to accommodate four monohydroxyethyl terephthalate (MHET) moieties of PET. Based on structural and site-directed mutagenesis experiments, the detailed process of PET degradation into MHET, terephthalic acid, and ethylene glycol is suggested. Moreover, other PETase candidates potentially having high PET-degrading activities are suggested based on phylogenetic tree analysis of 69 PETase-like proteins. Poly(ethylene terephthalate) (PET) is a widely used plastic and its accumulation in the environment has become global problem. Here the authors report the crystal structure of a Ideonella sakaiensis PET-degrading enzyme and propose a molecular mechanism for PET degradation.
Subfields: Biomaterials, Industrial and Manufacturing Engineering, Pollution
View Paper: https://www.semanticscholar.org/paper/7d03cb30ac2e858be3d4008dbe80defc9c2ffe71
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Citations in the corpus
- Enhanced Poly(ethylene terephthalate) Hydrolase Activity by Protein Engineering (2018, background): “This amino acid might function somewhat like the two inherent substrate phenyl ring-binding residues (W156/W130) that have been reported in PETase structural studies [28,35].”
- Characterization and engineering of a plastic-degrading aromatic polyesterase (2018, background): “(32) published a study with an R132G/S160A mutant (R132 and S160 in the numbering here) that was able to accommodate monomeric ligands, alongside the publication of another PETase structure soon after (33).”