8YTU
Mipa-PETase from Micromonospora pattaloongensis
Summary for 8YTU
Entry DOI | 10.2210/pdb8ytu/pdb |
Descriptor | cutinase, 1,2-ETHANEDIOL, GLYCEROL, ... (4 entities in total) |
Functional Keywords | pet hydrolase, hydrolase |
Biological source | Micromonospora pattaloongensis |
Total number of polymer chains | 3 |
Total formula weight | 84004.52 |
Authors | |
Primary citation | Seo, H.,Hong, H.,Park, J.,Lee, S.H.,Ki, D.,Ryu, A.,Sagong, H.Y.,Kim, K.J. Landscape profiling of PET depolymerases using a natural sequence cluster framework. Science, 387:eadp5637-eadp5637, 2025 Cited by PubMed Abstract: Enzymes capable of breaking down polymers have been identified from natural sources and developed for industrial use in plastic recycling. However, there are many potential starting points for enzyme optimization that remain unexplored. We generated a landscape of 170 lineages of 1894 polyethylene terephthalate depolymerase (PETase) candidates and performed profiling using sampling approaches with features associated with PET-degrading capabilities. We identified three promising yet unexplored PETase lineages and two potent PETases, Mipa-P and Kubu-P. An engineered variant of Kubu-P outperformed benchmarks in terms of PET depolymerization in harsh environments, such as those with high substrate load and ethylene glycol as the solvent. PubMed: 39745946DOI: 10.1126/science.adp5637 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.34 Å) |
Structure validation
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