8C65
Crystal structure of cutinase AdCut from Acidovorax delafieldii (PBS depolymerase)
Summary for 8C65
| Entry DOI | 10.2210/pdb8c65/pdb |
| Descriptor | PBS(A) depolymerase (2 entities in total) |
| Functional Keywords | cutinase, pet, pbs, hydrolase |
| Biological source | Acidovorax delafieldii |
| Total number of polymer chains | 2 |
| Total formula weight | 58756.96 |
| Authors | |
| Primary citation | Clark, M.,Tornesakis, K.,Konig, G.,Zahn, M.,Lichtenstein, B.R.,Pickford, A.R.,Cox, P.A. Understanding the Catalytic Efficiency of Two Polyester Degrading Enzymes: An Experimental and Theoretical Investigation. Acs Omega, 9:44724-44733, 2024 Cited by PubMed Abstract: The discovery of novel plastic degrading enzymes commonly relies on comparing features of the primary sequence to those of known plastic degrading enzymes. However, this approach cannot always guarantee success. This is exemplified by the different degradation rates of the two polymers poly(ethylene terephthalate) (PET) and polybutylene succinate (PBS) by two hydrolases: PETase from and Cut from . Despite the enzymes showing a very high sequence identity of 82%, PETase shows significant hydrolysis activity for both polymers, whereas Cut only shows significant hydrolysis activity for PBS. By solving the structure of Cut using X-ray crystallography, and using this as the basis for computer simulations, comparisons are made between the differences in the calculated binding geometries and the catalytic results obtained from biochemical experiments. The results reveal that the low activity of Cut toward PET can be explained by the low sampling of the productive conformation observed in the simulations. While the active site serine in PETase can closely encounter the PET carbonyl carbon, in Cut it cannot: a feature that can be attributed to the shape of the catalytic binding pocket. These results yield an important insight into the design requirements for novel plastic degrading enzymes, as well as showing that computational methods can be used as a valuable tool in understanding the molecular basis for different hydrolysis activities in homologous polyesterase enzymes. PubMed: 39524671DOI: 10.1021/acsomega.4c06528 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.491 Å) |
Structure validation
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