7YM9

Crystal structure of a PET hydrolase from Cryptosporangium aurantiacum

7YM9 の概要

• エントリーDOI: 10.2210/pdb7ym9/pdb
• 分子名称: Poly(ethylene terephthalate) hydrolase, MALONATE ION (3 entities in total)
• 機能のキーワード: poly(ethylene terephthalate) hydrolase, esterase, hydrolase
• 由来する生物種: Cryptosporangium aurantiacum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58132.93

構造登録者

Hong, H.,Ki, D.,Kim, K.-J. (登録日: 2022-07-28, 公開日: 2023-07-12, 最終更新日: 2024-11-06)

主引用文献

Hong, H.,Ki, D.,Seo, H.,Park, J.,Jang, J.,Kim, K.J.
Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties.
Nat Commun, 14:4556-4556, 2023

PubMed Abstract: Excessive polyethylene terephthalate (PET) waste causes a variety of problems. Extensive research focused on the development of superior PET hydrolases for PET biorecycling has been conducted. However, template enzymes employed in enzyme engineering mainly focused on IsPETase and leaf-branch compost cutinase, which exhibit mesophilic and thermophilic hydrolytic properties, respectively. Herein, we report a PET hydrolase from Cryptosporangium aurantiacum (CaPETase) that exhibits high thermostability and remarkable PET degradation activity at ambient temperatures. We uncover the crystal structure of CaPETase, which displays a distinct backbone conformation at the active site and residues forming the substrate binding cleft, compared with other PET hydrolases. We further develop a CaPETase variant that exhibits robust thermostability with a T of 83.2 °C and 41.7-fold enhanced PET hydrolytic activity at 60 °C compared with CaPETase. CaPETase almost completely decompose both transparent and colored post-consumer PET powder at 55 °C within half a day in a pH-stat bioreactor.

PubMed: 37507390
DOI: 10.1038/s41467-023-40233-w

実験手法

X-RAY DIFFRACTION (1.34 Å)