Structural and Biophysical Characterization of EppA
MetadataShow full item record
Ethylenediaminetetraacetate, better known as EDTA, is a chemically stable compound whose widespread use has led to its persistence in the environment as potentially toxic EDTA-metal complexes. Being a ubiquitous environmental pollutant, finding a means by which we can clean up EDTA pollution in the environment is imperative. One way to remove EDTA is through bioremediation in which a unique microbial process is harnessed, such as the epp-emo pathway from Chelativorans sp. BNC1. To these ends, we characterized the relationship between the structure and function of EppA, an EDTA-binding periplasmic protein.To obtain the molecular structure of EppA, we crystallized the protein and analyzed the structure using X-ray diffraction. We then used molecular docking to dock EDTA and chemically related chelators to the structure, showing that they bind with EppA’s putative ligand-binding cleft. To confirm their binding experimentally, isothermal titration calorimetry was used. EppA’s high affinity for chemically similar chelators suggests that other proteins further down the catabolic pathway may be useful for degrading a wider range of chelators than previously thought or can otherwise be engineered to do so. This makes the epp-emo EDTA-degradation pathway of Chelativorans sp. BNC1 a powerful tool for combating pollution.