Structure of the Plastic-degrading Ideonella Sakaiensis MHETase Bound to a Substrate

Overview

Journal Nat Commun

Specialty Biology

Date 2019 Apr 14

PMID 30979881

Citations 98

Authors

Gottfried J Palm

Lukas Reisky

Dominique Bottcher

Henrik Muller

Emil A P Michels

Miriam C Walczak

Leona Berndt

Manfred S Weiss

Uwe T Bornscheuer

Gert Weber

Affiliations

Soon will be listed here.

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.

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