8BRB

Polyester Hydrolase Leipzig 7 (PHL7) bound to terephthalic acid (TPA)

8BRB の概要

• エントリーDOI: 10.2210/pdb8brb/pdb
• 分子名称: Polyester Hydrolase Leipzig 7 (PHL-7), catalysis-deficient S131A mutant, terephthalic acid, DIMETHYL SULFOXIDE, ... (4 entities in total)
• 機能のキーワード: petase, cutinase, polyethylene terephthalate, hydrolase, terephthalic acid, tpa, polyester hydrolase
• 由来する生物種: unidentified
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58569.05

構造登録者

Richter, P.K.,Strater, N. (登録日: 2022-11-22, 公開日: 2023-04-19, 最終更新日: 2024-11-06)

主引用文献

Richter, P.K.,Blazquez-Sanchez, P.,Zhao, Z.,Engelberger, F.,Wiebeler, C.,Kunze, G.,Frank, R.,Krinke, D.,Frezzotti, E.,Lihanova, Y.,Falkenstein, P.,Matysik, J.,Zimmermann, W.,Strater, N.,Sonnendecker, C.
Structure and function of the metagenomic plastic-degrading polyester hydrolase PHL7 bound to its product.
Nat Commun, 14:1905-1905, 2023

PubMed Abstract: The recently discovered metagenomic-derived polyester hydrolase PHL7 is able to efficiently degrade amorphous polyethylene terephthalate (PET) in post-consumer plastic waste. We present the cocrystal structure of this hydrolase with its hydrolysis product terephthalic acid and elucidate the influence of 17 single mutations on the PET-hydrolytic activity and thermal stability of PHL7. The substrate-binding mode of terephthalic acid is similar to that of the thermophilic polyester hydrolase LCC and deviates from the mesophilic IsPETase. The subsite I modifications L93F and Q95Y, derived from LCC, increased the thermal stability, while exchange of H185S, derived from IsPETase, reduced the stability of PHL7. The subsite II residue H130 is suggested to represent an adaptation for high thermal stability, whereas L210 emerged as the main contributor to the observed high PET-hydrolytic activity. Variant L210T showed significantly higher activity, achieving a degradation rate of 20 µm h with amorphous PET films.

PubMed: 37019924
DOI: 10.1038/s41467-023-37415-x

実験手法

X-RAY DIFFRACTION (1.7 Å)