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7YM9

Crystal structure of a PET hydrolase from Cryptosporangium aurantiacum

Summary for 7YM9
Entry DOI10.2210/pdb7ym9/pdb
DescriptorPoly(ethylene terephthalate) hydrolase, MALONATE ION (3 entities in total)
Functional Keywordspoly(ethylene terephthalate) hydrolase, esterase, hydrolase
Biological sourceCryptosporangium aurantiacum
Total number of polymer chains2
Total formula weight58132.93
Authors
Hong, H.,Ki, D.,Kim, K.-J. (deposition date: 2022-07-28, release date: 2023-07-12, Last modification date: 2024-11-06)
Primary citationHong, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.34 Å)
Structure validation

238582

数据于2025-07-09公开中

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