9KTI
CryoEM structure of a 2,3-hydroxycinnamic acid 1,2-dioxygenase MhpB in substrate bound form
This is a non-PDB format compatible entry.
Summary for 9KTI
| Entry DOI | 10.2210/pdb9kti/pdb |
| EMDB information | 62561 |
| Descriptor | 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase, FE (II) ION, 3-[2,3-bis(oxidanyl)phenyl]propanoic acid (3 entities in total) |
| Functional Keywords | 2, 3-hydroxycinnamic acid 1, 2-dioxygenase, biosynthetic protein |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 10 |
| Total formula weight | 344689.79 |
| Authors | |
| Primary citation | Dong, X.,Xu, M.,Wu, M.,Wang, Y.,Cheng, X.,Jiang, W.,Zheng, D.,Omar, A.H.,Cheng, Y.,Li, A.,Ma, L.,Xing, Q. Structural and catalytic insights into MhpB: A dioxygenase enzyme for degrading catecholic pollutants. J Hazard Mater, 488:137431-137431, 2025 Cited by PubMed Abstract: The 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. PubMed: 39892151DOI: 10.1016/j.jhazmat.2025.137431 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.59 Å) |
Structure validation
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