6QGB

Crystal structure of Ideonella sakaiensis MHETase bound to benzoic acid

Summary for 6QGB

• Entry DOI: 10.2210/pdb6qgb/pdb
• Descriptor: Mono(2-hydroxyethyl) terephthalate hydrolase, BENZOIC ACID, CALCIUM ION, ... (7 entities in total)
• Functional Keywords: plastic-degrading hydrolase, alpha/beta hydrolase fold, i. sakaiensis catalytic triad, hydrolase
• Biological source: Ideonella sakaiensis
• Total number of polymer chains: 6
• Total formula weight: 379400.40

Authors

Palm, G.J.,Reisky, L.,Boettcher, D.,Mueller, H.,Michels, E.A.P.,Walczak, C.,Berndt, L.,Weiss, M.S.,Bornscheuer, U.T.,Weber, G. (deposition date: 2019-01-10, release date: 2019-04-03, Last modification date: 2024-10-23)

Primary citation

Palm, G.J.,Reisky, L.,Bottcher, D.,Muller, H.,Michels, E.A.P.,Walczak, M.C.,Berndt, L.,Weiss, M.S.,Bornscheuer, U.T.,Weber, G.
Structure of the plastic-degrading Ideonella sakaiensis MHETase bound to a substrate.
Nat Commun, 10:1717-1717, 2019

PubMed 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.

PubMed: 30979881
DOI: 10.1038/s41467-019-09326-3

Experimental method

X-RAY DIFFRACTION (2.2 Å)