8JMO

Structure of a leaf-branch compost cutinase, ICCG in complex with 4-((4-Hydroxybutoxy)carbonyl)benzoic acid

Summary for 8JMO

• Entry DOI: 10.2210/pdb8jmo/pdb
• Descriptor: Leaf-branch compost cutinase, CALCIUM ION, 4-(4-oxidanylbutoxycarbonyl)benzoic acid, ... (4 entities in total)
• Functional Keywords: petase, cutinase, enzyme engineering, pbat degradation, hydrolase
• Biological source: unidentified prokaryotic organism
• Total number of polymer chains: 2
• Total formula weight: 56188.99

Authors

Yang, Y.,Xue, T.,Zheng, Y.,Cheng, S.,Guo, R.-T.,Chen, C.-C. (deposition date: 2023-06-05, release date: 2023-11-29, Last modification date: 2024-11-13)

Primary citation

Yang, Y.,Cheng, S.,Zheng, Y.,Xue, T.,Huang, J.W.,Zhang, L.,Yang, Y.,Guo, R.T.,Chen, C.C.
Remodeling the polymer-binding cavity to improve the efficacy of PBAT-degrading enzyme.
J Hazard Mater, 464:132965-132965, 2023

PubMed Abstract: Poly(butylene adipate-co-terephthalate) (PBAT) is among the most widely applied synthetic polyesters that are utilized in the packaging and agricultural industries, but the accumulation of PBAT wastes has posed a great burden to ecosystems. Using renewable enzymes to decompose PBAT is an eco-friendly solution to tackle this problem. Recently, we demonstrated that cutinase is the most effective PBAT-degrading enzyme and that an engineered cutinase termed TfCut-DM could completely decompose PBAT film to terephthalate (TPA). Here, we report crystal structures of a variant of leaf compost cutinase in complex with soluble fragments of PBAT, including BTa and TaBTa. In the TaBTa complex, one TPA moiety was located at a polymer-binding site distal to the catalytic center that has never been experimentally validated. Intriguingly, the composition of the distal TPA-binding site shows higher diversity relative to the one proximal to the catalytic center in various cutinases. We thus modified the distal TPA-binding site of TfCut-DM and obtained variants that exhibit higher activity. Notably, the time needed to completely degrade the PBAT film to TPA was shortened to within 24 h by TfCut-DM Q132Y (5813 mol per mol protein). Taken together, the structural information regarding the substrate-binding behavior of PBAT-degrading enzymes could be useful guidance for direct enzyme engineering.

PubMed: 37979420
DOI: 10.1016/j.jhazmat.2023.132965

Experimental method

X-RAY DIFFRACTION (1.95 Å)