9kti
From Proteopedia
CryoEM structure of a 2,3-hydroxycinnamic acid 1,2-dioxygenase MhpB in substrate bound form
Structural highlights
FunctionMHPB_ECOLI Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively.[1] [2] Publication Abstract from PubMedThe increasing environmental pollution from persistent aromatic compounds requires effective biodegradation strategies. In this study, we focused on MhpB, an extradiol dioxygenase (EDO) from Escherichia coli. It is known for its role in the degradation of catechols, key intermediates in the degradation of aromatic compounds. We report the high-resolution structure of MhpB determined by cryo-electron microscopy, revealing a decameric conformation with the catalytic chamber at the side. The structure-based analysis allowed us to investigate the substrate-enzyme interaction and the substrate selectivity, which are crucial for its catalytic function. Site-directed mutagenesis was used to modulate the in vitro and in vivo substrate preference of MhpB, enhancing its potential for industrial applications in pollutant degradation. The study provides insight into the mechanism of the enzyme and paves the way for the development of engineered EDOs for environmental remediation of aromatic pollutants. Structural and catalytic insights into MhpB: A dioxygenase enzyme for degrading catecholic pollutants.,Dong X, Xu M, Wu M, Wang Y, Cheng X, Jiang W, Zheng D, Omar AH, Cheng Y, Li A, Ma L, Xing Q J Hazard Mater. 2025 Jan 28;488:137431. doi: 10.1016/j.jhazmat.2025.137431. PMID:39892151[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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