Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

9W68

Crystal structural of dsPETase05

Summary for 9W68
Entry DOI10.2210/pdb9w68/pdb
DescriptorPETase (2 entities in total)
Functional Keywordspolyethylene terephthalate, petase, plastic waste recovery, lyase
Biological sourceBacteria Latreille et al. 1825
Total number of polymer chains1
Total formula weight28815.39
Authors
Wang, Y.,Xu, B. (deposition date: 2025-08-03, release date: 2026-07-08)
Primary citationZhang, 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: 41548779
DOI: 10.1016/j.ijbiomac.2026.150252
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.93 Å)
Structure validation

256789

PDB entries from 2026-07-22

PDB statisticsPDBj update infoContact PDBjnumon