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

Gottfried J. Palm, Lukas Reisky, Dominique Böttcher, Henrik Müller, Emil A. P. Michels, Miriam C. Walczak, Leona Berndt, Manfred S. Weiss, Uwe T. Bornscheuer () and Gert Weber ()
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Gottfried J. Palm: University of Greifswald
Lukas Reisky: University of Greifswald
Dominique Böttcher: University of Greifswald
Henrik Müller: University of Greifswald
Emil A. P. Michels: University of Greifswald
Miriam C. Walczak: University of Greifswald
Leona Berndt: University of Greifswald
Manfred S. Weiss: Helmholtz-Zentrum Berlin für Materialien und Energie
Uwe T. Bornscheuer: University of Greifswald
Gert Weber: University of Greifswald

Nature Communications, 2019, vol. 10, issue 1, 1-10

Abstract: Abstract 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.

Date: 2019
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DOI: 10.1038/s41467-019-09326-3

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