AlphaFold-predicted structures of selected de novo designed PET hydrolases in comparison with their naturally evolved counterparts. (IMAGE)

Higher Education Press

AlphaFold-predicted structures of selected de novo designed PET hydrolases in comparison with their naturally evolved counterparts.

Caption

(a) momi120-103. (b) RsPETase1. (c) Structural superposition of RsPETase1 (pale cyan) and the precursor wild-type LCC (wheat; Protein Data Bank (PDB) code: 4EB0) used for its design. (d) Crystal structure of the fungal PET hydrolase Humicola insolens cutinase (HiC; PDB code: 4OYY). The side chains of the catalytic triad residues are shown as sticks in (a), (b), and (d).

Credit

Ren Wei, Uwe T. Bornscheuer

Usage Restrictions

Credit must be given to the creator. Only noncommercial uses of the work are permitted. No derivatives or adaptations of the work are permitted.

License

CC BY-NC-ND

Disclaimer: AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert system.