[논문]Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate

Palm, Gottfried J.; Reisky, Lukas; Bö; ttcher, Dominique; Mü; ller, Henrik; Michels, Emil A. P.; Walczak, Miriam C.; Berndt, Leona; Weiss, Manfred S.; Bornscheuer, Uwe T.; Weber, Gert

doi:10.1038/s41467-019-09326-3

Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate 원문보기

Nature communications, v.10 no.1, 2019년, pp.1717 -

Palm, Gottfried J. (Molecular Structural Biology, University of Greifswald, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany) , Reisky, Lukas (Biotechnology & Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany) , Böttcher, Dominique (Biotechnology & Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany) , Müller, Henrik (Biotechnology & Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany) , Michels, Emil A. P. (Molecular Structural Biology, University of Greifswald, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany) , Walczak, Miriam C. (Biotechnology & Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany) , Berndt, Leona (Molecular Structural Biology, University of Greifswald, Felix-Hausdorff-Str. 4, 17487 Greifswald, Germany) , Weiss, Manfred S. (Macromolecular Crystallography, Helmholtz-Zentrum Berlin fü) , Bornscheuer, Uwe T. (r Materialien und Energie, Albert-Einstein-Straße15, 12489 Berlin, Germany) , Weber, Gert (Biotechnology & Enzyme Catalysis, University of Greifswald, Felix-Hausdorff-Str. 4, 1)

Abstract ▼ AI-Helper

The extreme durability of polyethylene terephthalate (PET) debris has rendered it a long-term environmental burden. At the same time, current recycling efforts still lack sustainability. Two recently discovered bacterial enzymes that specifically degrade PET represent a promising solution. First, Ideonella sakaiensis PETase, a structurally well-characterized consensus α/β-hydrolase fold enzyme, converts PET to mono-(2-hydroxyethyl) terephthalate (MHET). MHETase, the second key enzyme, hydrolyzes MHET to the PET educts terephthalate and ethylene glycol. Here, we report the crystal structures of active ligand-free MHETase and MHETase bound to a nonhydrolyzable MHET analog. MHETase, which is reminiscent of feruloyl esterases, possesses a classic α/β-hydrolase domain and a lid domain conferring substrate specificity. In the light of structure-based mapping of the active site, activity assays, mutagenesis studies and a first structure-guided alteration of substrate specificity towards bis-(2-hydroxyethyl) terephthalate (BHET) reported here, we anticipate MHETase to be a valuable resource to further advance enzymatic plastic degradation.Plastic polymer PET degrading enzymes are of great interest for achieving sustainable plastics recycling. Here, the authors present the crystal structures of the plastic degrading bacterial enzymes PETase, MHETase in its apo-form and MHETase bound to a non-hydrolyzable substrate analog.

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Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate 원문보기

Abstract ▼ AI-Helper

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