9l1w

3-phenylpropionate bound dioxygenase HcaE-HcaF

spinqualitylabelsall models 9l1w, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9l1w is a 6 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.1Å Ligands: FE2, FES, HCI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HCAE_ECOLI Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively. Publication Abstract from PubMed 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 approximately 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. Structure-guided engineering of a Rieske-type aromatic dioxygenase for enhanced consumption of 3-phenylpropionic acid in Escherichia coli.,Jiang W, Wu M, Gong Z, Han L, Cheng X, Tang X, Yu X, Dong X, Cheng Y, Ma L, Xing Q J Hazard Mater. 2025 Jul 5;491:137954. doi: 10.1016/j.jhazmat.2025.137954. Epub , 2025 Mar 19. PMID:40120277 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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