5XJH

Crystal structure of PETase from Ideonella sakaiensis

Summary for 5XJH

• Entry DOI: 10.2210/pdb5xjh/pdb
• Descriptor: Poly(ethylene terephthalate) hydrolase (2 entities in total)
• Functional Keywords: hydrolase
• Biological source: Ideonella sakaiensis
• Total number of polymer chains: 1
• Total formula weight: 31490.91

Authors

Joo, S.,Kim, K.-J. (deposition date: 2017-05-01, release date: 2018-02-14, Last modification date: 2024-10-30)

Primary citation

Joo, S.,Cho, I.J.,Seo, H.,Son, H.F.,Sagong, H.-Y.,Shin, T.J.,Choi, S.Y.,Lee, S.Y.,Kim, K.-J.
Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation.
Nat Commun, 9:382-382, 2018

PubMed 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 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.

PubMed: 29374183
DOI: 10.1038/s41467-018-02881-1

Experimental method

X-RAY DIFFRACTION (1.54 Å)