8GU5

Wild type poly(ethylene terephthalate) hydrolase

8GU5 の概要

• エントリーDOI: 10.2210/pdb8gu5/pdb
• 分子名称: Poly(ethylene terephthalate) hydrolase (2 entities in total)
• 機能のキーワード: petase, lyase, hydrolase
• 由来する生物種: Ideonella sakaiensis (strain NBRC 110686 / TISTR 2288 / 201-F6)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28782.92

構造登録者

Xiao, Y.J.,Wang, Z.F. (登録日: 2022-09-09, 公開日: 2022-11-30, 最終更新日: 2024-11-20)

主引用文献

Chen, Z.,Duan, R.,Xiao, Y.,Wei, Y.,Zhang, H.,Sun, X.,Wang, S.,Cheng, Y.,Wang, X.,Tong, S.,Yao, Y.,Zhu, C.,Yang, H.,Wang, Y.,Wang, Z.
Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin.
Nat Commun, 13:7138-7138, 2022

PubMed Abstract: The process of recycling poly(ethylene terephthalate) (PET) remains a major challenge due to the enzymatic degradation of high-crystallinity PET (hcPET). Recently, a bacterial PET-degrading enzyme, PETase, was found to have the ability to degrade the hcPET, but with low enzymatic activity. Here we present an engineered whole-cell biocatalyst to simulate both the adsorption and degradation steps in the enzymatic degradation process of PETase to achieve the efficient degradation of hcPET. Our data shows that the adhesive unit hydrophobin and degradation unit PETase are functionally displayed on the surface of yeast cells. The turnover rate of the whole-cell biocatalyst toward hcPET (crystallinity of 45%) dramatically increases approximately 328.8-fold compared with that of purified PETase at 30 °C. In addition, molecular dynamics simulations explain how the enhanced adhesion can promote the enzymatic degradation of PET. This study demonstrates engineering the whole-cell catalyst is an efficient strategy for biodegradation of PET.

PubMed: 36414665
DOI: 10.1038/s41467-022-34908-z

実験手法

X-RAY DIFFRACTION (2.02 Å)