8b4u

The crystal structure of PET46, a PETase enzyme from Candidatus bathyarchaeota

spinqualitylabelsall models 8b4u, resolution 1.71Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8b4u is a 1 chain structure with sequence from Candidatus Bathyarchaeota archaeon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.71Å Ligands: CL, EDO, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A497NK85_9ARCH Publication Abstract from PubMed Polyethylene terephthalate (PET) is a commodity polymer known to globally contaminate marine and terrestrial environments. Today, around 80 bacterial and fungal PET-active enzymes (PETases) are known, originating from four bacterial and two fungal phyla. In contrast, no archaeal enzyme had been identified to degrade PET. Here we report on the structural and biochemical characterization of PET46 (RLI42440.1), an archaeal promiscuous feruloyl esterase exhibiting degradation activity on semi-crystalline PET powder comparable to IsPETase and LCC (wildtypes), and higher activity on bis-, and mono-(2-hydroxyethyl) terephthalate (BHET and MHET). The enzyme, found by a sequence-based metagenome search, is derived from a non-cultivated, deep-sea Candidatus Bathyarchaeota archaeon. Biochemical characterization demonstrated that PET46 is a promiscuous, heat-adapted hydrolase. Its crystal structure was solved at a resolution of 1.71 A. It shares the core alpha/beta-hydrolase fold with bacterial PETases, but contains a unique lid common in feruloyl esterases, which is involved in substrate binding. Thus, our study widens the currently known diversity of PET-hydrolyzing enzymes, by demonstrating PET depolymerization by a plant cell wall-degrading esterase. An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate.,Perez-Garcia P, Chow J, Costanzi E, Gurschke M, Dittrich J, Dierkes RF, Molitor R, Applegate V, Feuerriegel G, Tete P, Danso D, Thies S, Schumacher J, Pfleger C, Jaeger KE, Gohlke H, Smits SHJ, Schmitz RA, Streit WR Commun Chem. 2023 Sep 11;6(1):193. doi: 10.1038/s42004-023-00998-z. PMID:37697032 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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