6QGA

Crystal structure of Ideonella sakaiensis MHETase bound to the non-hydrolyzable ligand MHETA

6QGA の概要

• エントリーDOI: 10.2210/pdb6qga/pdb
• 分子名称: Mono(2-hydroxyethyl) terephthalate hydrolase, 4-(2-hydroxyethylcarbamoyl)benzoic acid, SULFATE ION, ... (7 entities in total)
• 機能のキーワード: plastic-degrading hydrolase, alpha/beta hydrolase fold, i. sakaiensis catalytic triad, hydrolase
• 由来する生物種: Ideonella sakaiensis
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 380736.02

構造登録者

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. (登録日: 2019-01-10, 公開日: 2019-04-03, 最終更新日: 2024-11-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)