8hgw

Crystal structure of MehpH in complex with MBP

spinqualitylabelsall models 8hgw, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8hgw is a 4 chain structure with sequence from Gordonia sp. P8219. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8000116Å Ligands: 1BO, PHT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2MHH5_9ACTN Publication Abstract from PubMed 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. Molecular insights into the catalytic mechanism of plasticizer degradation by a monoalkyl phthalate hydrolase.,Chen Y, Wang Y, Xu Y, Sun J, Yang L, Feng C, Wang J, Zhou Y, Zhang ZM, Wang Y Commun Chem. 2023 Mar 1;6(1):45. doi: 10.1038/s42004-023-00846-0. PMID:36859434 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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