8HGW
Crystal structure of MehpH in complex with MBP
Summary for 8HGW
| Entry DOI | 10.2210/pdb8hgw/pdb |
| Descriptor | Monoalkyl phthalate hydrolase, 1-BUTANOL, PHTHALIC ACID (3 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Gordonia sp. P8219 |
| Total number of polymer chains | 4 |
| Total formula weight | 126732.31 |
| Authors | Zhang, Z.M.,Wang, Y.J.,Chen, Y.B. (deposition date: 2022-11-15, release date: 2023-03-15, Last modification date: 2024-10-30) |
| 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 Cited by 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: 36859434DOI: 10.1038/s42004-023-00846-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.80001173333 Å) |
Structure validation
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