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

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…

• HZ
  Humboldt-Universität zu Berlin
• FU
  Freie Universität Berlin
• HB
  Helmholtz-Zentrum Berlin für Materialien und Energie
• DE
  Deutsches Elektronen-Synchrotron
• L
  Leibniz-Gemeinschaft