9W68
Crystal structural of dsPETase05
Summary for 9W68
| Entry DOI | 10.2210/pdb9w68/pdb |
| Descriptor | PETase (2 entities in total) |
| Functional Keywords | polyethylene terephthalate, petase, plastic waste recovery, lyase |
| Biological source | Bacteria Latreille et al. 1825 |
| Total number of polymer chains | 1 |
| Total formula weight | 28815.39 |
| Authors | |
| Primary citation | Zhang, L.,Zhou, X.,Yuan, Y.,Li, H.,Li, J.,Zhou, Y.,Du, S.,Wang, Z.,Han, Y.,Fan, X.,Han, D.,Wang, L.,Zhu, C.,Ye, S.,Wang, Y.,Xu, B. Structural and functional characterization of dsPETase05 for the degradation of Polyethylene terephthalate. Int.J.Biol.Macromol., 343:150252-150252, 2026 Cited by PubMed Abstract: The enzymatic degradation of polyethylene terephthalate (PET) represents a promising sustainable strategy to address global plastic pollution. Among various plastic-degrading enzymes, PETase has been one of the most extensively studied and widely applied. Discovering novel PETase variants and elucidating their structure-function relationships are essential for developing more efficient enzymes. Here, we studied dsPETase05, a deep-sea PET hydrolase that was previously reported, which exhibits significantly enhanced PET degradation activity compared to the wild-type Ideonella sakaiensis PETase (IsPETase). This improvement was corroborated by atomic force microscopy (AFM) analysis of PET surface erosion and high-performance liquid chromatography (HPLC) quantification of hydrolysis products. We heterologously expressed and biochemically characterized dsPETase05, and resolved its crystal structure at 1.93 Å resolution. Structural analysis revealed that dsPETase05 adopts the typical α/β-hydrolase architecture found in PET-degrading enzymes, with distinctive amino acid substitutions near the catalytic triad that may contribute to its elevated activity. Our findings highlight the potential of marine-derived PETase for enzymatic plastic waste remediation and expand the repertoire of biocatalysts available for sustainable PET degradation. PubMed: 41548779DOI: 10.1016/j.ijbiomac.2026.150252 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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