7YME

Crystal structure of a PET hydrolase M9 variant from Cryptosporangium aurantiacum

Summary for 7YME

• Entry DOI: 10.2210/pdb7yme/pdb
• Descriptor: Poly(Ethylene terephthalate) hydrolase (2 entities in total)
• Functional Keywords: poly(ethylene terephthalate) hydrolase, esterase, hydrolase
• Biological source: Cryptosporangium aurantiacum
• Total number of polymer chains: 2
• Total formula weight: 66096.56

Authors

Ki, D.,Hong, H.,Kim, K.-J. (deposition date: 2022-07-28, release date: 2023-07-12, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.5 Å)