Title : Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation - Joo_2018_Nat.Commun_9_382 |
Author(s) : Joo S , Cho IJ , Seo H , Son HF , Sagong HY , Shin TJ , Choi SY , Lee SY , Kim KJ |
Ref : Nat Commun , 9 :382 , 2018 |
Abstract :
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 A 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. |
PubMedSearch : Joo_2018_Nat.Commun_9_382 |
PubMedID: 29374183 |
Gene_locus related to this paper: idesa-peth |
Inhibitor | Terephthalic-acid MHET |
Substrate | 2HE(MHET)4 2HE(MHET)2 HEMT MHET BHET Polyethylene-terephthalate |
Gene_locus | idesa-peth |
Family | Polyesterase-lipase-cutinase |
Structure | 5YNS 5XJH |
Chemical | Ethylene-glycol Terephthalic-acid |
Joo S, Cho IJ, Seo H, Son HF, Sagong HY, Shin TJ, Choi SY, Lee SY, Kim KJ (2018)
Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation
Nat Commun
9 :382
Joo S, Cho IJ, Seo H, Son HF, Sagong HY, Shin TJ, Choi SY, Lee SY, Kim KJ (2018)
Nat Commun
9 :382