Molecular analysis of the Escherichia coli ferric enterobactin receptor FepA.
نویسندگان
چکیده
منابع مشابه
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...
متن کاملPassive 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...
متن کاملpassive 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...
متن کاملRecognition 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...
متن کاملStereospecificity of the ferric enterobactin receptor of Escherichia coli K-12.
Synthetic enterobactin and enantioenterobactin (D-seryl enterobactin) have been examined for the ability to transport iron in Escherichia coli. Failure of the unnatural, D-serine-derived material to support growth of E. coli mutants indicates outer membrane receptor specificity for the naturally occurring complex having an L-seryl backbone and the delta-cis configuration of the Fe(III).catechol...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1990
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)77336-5