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Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation

Author

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  • Seongjoon Joo

    (Kyungpook National University)

  • In Jin Cho

    (Korea Advanced Institute of Science and Technology (KAIST))

  • Hogyun Seo

    (Kyungpook National University)

  • Hyeoncheol Francis Son

    (Kyungpook National University)

  • Hye-Young Sagong

    (Kyungpook National University)

  • Tae Joo Shin

    (Ulsan National Institute of Science and Technology)

  • So Young Choi

    (Korea Advanced Institute of Science and Technology (KAIST))

  • Sang Yup Lee

    (Korea Advanced Institute of Science and Technology (KAIST))

  • Kyung-Jin Kim

    (Kyungpook National University)

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.

Suggested Citation

  • Seongjoon Joo & In Jin Cho & Hogyun Seo & Hyeoncheol Francis Son & Hye-Young Sagong & Tae Joo Shin & So Young Choi & Sang Yup Lee & Kyung-Jin Kim, 2018. "Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-02881-1
    DOI: 10.1038/s41467-018-02881-1
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    Cited by:

    1. Hwaseok Hong & Dongwoo Ki & Hogyun Seo & Jiyoung Park & Jaewon Jang & Kyung-Jin Kim, 2023. "Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Trishnamoni Gautom & Dharmendra Dheeman & Colin Levy & Thomas Butterfield & Guadalupe Alvarez Gonzalez & Philip Roy & Lewis Caiger & Karl Fisher & Linus Johannissen & Neil Dixon, 2021. "Structural basis of terephthalate recognition by solute binding protein TphC," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
    3. Zhuozhi Chen & Rongdi Duan & Yunjie Xiao & Yi Wei & Hanxiao Zhang & Xinzhao Sun & Shen Wang & Yingying Cheng & Xue Wang & Shanwei Tong & Yunxiao Yao & Cheng Zhu & Haitao Yang & Yanyan Wang & Zefang Wa, 2022. "Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    4. P. Konstantin Richter & Paula Blázquez-Sánchez & Ziyue Zhao & Felipe Engelberger & Christian Wiebeler & Georg Künze & Ronny Frank & Dana Krinke & Emanuele Frezzotti & Yuliia Lihanova & Patricia Falken, 2023. "Structure and function of the metagenomic plastic-degrading polyester hydrolase PHL7 bound to its product," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    5. Erika Erickson & Japheth E. Gado & Luisana Avilán & Felicia Bratti & Richard K. Brizendine & Paul A. Cox & Raj Gill & Rosie Graham & Dong-Jin Kim & Gerhard König & William E. Michener & Saroj Poudel &, 2022. "Sourcing thermotolerant poly(ethylene terephthalate) hydrolase scaffolds from natural diversity," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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