Conformational rearrangements in the N-domain of Escherichia coli FepA during ferric enterobactin transport

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Aromatic components of two ferric enterobactin binding sites in Escherichia coli FepA.

Ferric enterobactin is a catecholate siderophore that binds with high affinity (Kd approximately 10-10 M) to the Escherichia coli outer membrane protein FepA. We studied the involvement of aromatic amino acids in its uptake by determining the binding affinities, kinetics and transport properties of site-directed mutants. We replaced seven aromatic residues (Y260, Y272, Y285, Y289, W297, Y309 an...

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Recognition and transport of ferric enterobactin in Escherichia coli.

The specificity of the outer membrane protein receptor for ferric enterobactin transport in Escherichia coli and the mechanism of enterobactin-mediated transport of ferric ions across the outer membrane have been studied. Transport kinetic and inhibition studies with ferric enterobactin and synthetic structural analogs have mapped the parts of the molecule important for receptor binding. The fe...

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Passive immunization by recombinant ferric enterobactin protein (FepA) from Escherichia coli O157

BACKGROUND AND OBJECTIVES Enterohemorrhagic Escherichia coli (EHEC) O157:H7 has been recognized as a major food borne pathogen responsible for frequent hemorrhagic colitis and hemolytic uremic syndrome in humans. Cattle are important reservoirs of E. coli O157:H7, in which the organism colonizes the intestinal tract and is shed in the feces. OBJECTIVE Vaccination of cattle has significant pot...

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passive immunization by recombinant ferric enterobactin protein (fepa) from escherichia coli o157.

background and objectives: enterohemorrhagic escherichia coli (ehec) o157:h7 has been recognized as a major food borne pathogen responsible for frequent hemorrhagic colitis and hemolytic uremic syndrome in humans. cattle are important reservoirs of e. coli o157:h7, in which the organism colonizes the intestinal tract and is shed in the feces. objective: vaccination of cattle has significant pot...

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Spectroscopic observations of ferric enterobactin transport.

We characterized the uptake of ferric enterobactin (FeEnt), the native Escherichia coli ferric siderophore, through its cognate outer membrane receptor protein, FepA, using a site-directed fluorescence methodology. The experiments first defined locations in FepA that were accessible to covalent modification with fluorescein maleimide (FM) in vivo; among 10 sites that we tested by substituting s...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 2020

ISSN: 0021-9258

DOI: 10.1074/jbc.ra119.011850