{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lewis KM"],"funding":["National Science Foundation"],"pagination":["E3940"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7312458"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["21(11)"],"pubmed_abstract":["The widespread use of synthetic aminopolycarboxylates, such as ethylenediaminetetraacetate (EDTA), as chelating agents has led to their contamination in the environment as stable metal-chelate complexes. Microorganisms can transport free EDTA, but not metal-EDTA complexes, into cells for metabolism. An ABC-type transporter for free EDTA uptake in <i>Chelativorans</i> sp. BNC1 was investigated to understand the mechanism of the ligand selectivity. We solved the X-ray crystal structure of the periplasmic EDTA-binding protein (EppA) and analyzed its structure-function relations through isothermal titration calorimetry, site-directed mutagenesis, molecular docking, and quantum chemical analysis. EppA had high affinities for EDTA and other aminopolycarboxylates, which agrees with structural ana"],"journal":["International journal of molecular sciences"],"pubmed_title":["The Structural Basis of the Binding of Various Aminopolycarboxylates by the Periplasmic EDTA-Binding Protein EppA from <i>Chelativorans</i> sp. BNC1."],"pmcid":["PMC7312458"],"funding_grant_id":["CHE 1804699"],"pubmed_authors":["Lewis KM","Youn B","Xun L","Sattler SA","Kang C","Greene CL"],"additional_accession":[]},"is_claimable":false,"name":"The Structural Basis of the Binding of Various Aminopolycarboxylates by the Periplasmic EDTA-Binding Protein EppA from <i>Chelativorans</i> sp. BNC1.","description":"The widespread use of synthetic aminopolycarboxylates, such as ethylenediaminetetraacetate (EDTA), as chelating agents has led to their contamination in the environment as stable metal-chelate complexes. Microorganisms can transport free EDTA, but not metal-EDTA complexes, into cells for metabolism. An ABC-type transporter for free EDTA uptake in <i>Chelativorans</i> sp. BNC1 was investigated to understand the mechanism of the ligand selectivity. We solved the X-ray crystal structure of the periplasmic EDTA-binding protein (EppA) and analyzed its structure-function relations through isothermal titration calorimetry, site-directed mutagenesis, molecular docking, and quantum chemical analysis. EppA had high affinities for EDTA and other aminopolycarboxylates, which agrees with structural ana","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 May","modification":"2026-05-02T18:25:02.602Z","creation":"2020-07-01T07:05:58Z"},"accession":"S-EPMC7312458","cross_references":{"pubmed":["32486296"],"doi":["10.3390/ijms21113940"]}}