8HGV

Crystal structure of monoalkyl phthalate hydrolase MehpH

Summary for 8HGV

• Entry DOI: 10.2210/pdb8hgv/pdb
• Descriptor: Monoethylhexylphthalate hydrolase (2 entities in total)
• Functional Keywords: hydrolase
• Biological source: Gordonia sp. P8219
• Total number of polymer chains: 2
• Total formula weight: 62736.41

Authors

Zhang, Z.M.,Wang, Y.J.,Chen, Y.B. (deposition date: 2022-11-15, release date: 2023-03-15, Last modification date: 2023-09-06)

Primary citation

Chen, Y.,Wang, Y.,Xu, Y.,Sun, J.,Yang, L.,Feng, C.,Wang, J.,Zhou, Y.,Zhang, Z.M.,Wang, Y.
Molecular insights into the catalytic mechanism of plasticizer degradation by a monoalkyl phthalate hydrolase.
Commun Chem, 6:45-45, 2023

PubMed Abstract: Phthalate acid esters (PAEs), a group of xenobiotic compounds used extensively as plasticizers, have attracted increasing concern for adverse effects to human health and the environment. Microbial degradation relying on PAE hydrolases is a promising treatment. However, only a limited number of PAE hydrolases were characterized to date. Here we report the structures of MehpH, a monoalkyl phthalate (MBP) hydrolase that catalyzes the reaction of MBP to phthalic acid and the corresponding alcohol, in apo and ligand-bound form. The structures reveal a positively-charged catalytic center, complementary to the negatively-charged carboxyl group on MBP, and a penetrating tunnel that serves as exit of alcohol. The study provides a first glimpse into the enzyme-substrate binding model for PAE hydrolases, leading strong support to the development of better enzymes in the future.

PubMed: 36859434
DOI: 10.1038/s42004-023-00846-0

Experimental method

X-RAY DIFFRACTION (2.30006253403 Å)