9L1W
3-phenylpropionate bound dioxygenase HcaE-HcaF
Summary for 9L1W
| Entry DOI | 10.2210/pdb9l1w/pdb |
| Related | 8K0A |
| EMDB information | 62756 |
| Descriptor | 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha, 3-phenylpropionate/cinnamic acid dioxygenase subunit beta, FE (II) ION, ... (5 entities in total) |
| Functional Keywords | rieske-type aromatic dioxygenase, electron transport |
| Biological source | Escherichia coli K-12 More |
| Total number of polymer chains | 6 |
| Total formula weight | 216471.40 |
| Authors | Jiang, W.X.,Wu, M.,Cheng, X.Q.,Ma, L.X.,Xing, Q. (deposition date: 2024-12-16, release date: 2025-12-10) |
| Primary citation | Jiang, W.,Wu, M.,Gong, Z.,Han, L.,Cheng, X.,Tang, X.,Yu, X.,Dong, X.,Cheng, Y.,Ma, L.,Xing, Q. Structure-guided engineering of a Rieske-type aromatic dioxygenase for enhanced consumption of 3-phenylpropionic acid in Escherichia coli. J Hazard Mater, 491:137954-137954, 2025 Cited by PubMed Abstract: Industrial derived aromatic hydrocarbons are persistent environmental pollutants due to their chemical stability, posing both ecological and health risks. Rieske-type aromatic dioxygenases (RDOs), known for their role in dihydroxylation of aromatic rings, play a pivotal role in microbial consumption and degradation of such compounds. While the industrial application of these enzymes has been impeded by their instability and low biodegradation rate. In this study, we focused on optimization and application of the Rieske-type dioxygenase HcaEF from Escherichia coli (E. coli) K-12, which initializes the degradation of 3-phenylpropionic acid (3-PP) and cinnamic acid (CI). Using cryo-electron microscopy (cryo-EM), we determined the high-resolution structures of the apo-form and 3-PP bound form of HcaEF, revealing key insights into substrate specificity and thermal stability. Leveraging these structural insights, we engineered a Q73I variant of HcaEF. Upon introduction of this mutation, the turnover rate increased from 29.6 % to 43.8 %, showing ∼50 % improvement. Overexpression of this variant in E. coli K-12 significantly enhanced the strain's ability to utilize 3-PP, demonstrating the potential for microbial engineering in environmental bioremediation and industrial applications. Our findings not only deepen the understanding of substrate recognition in RDOs, but also pave the way for developing high-efficiency enzymes for aromatic compound bio-utilization. PubMed: 40120277DOI: 10.1016/j.jhazmat.2025.137954 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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