Mutations in the Escherichia coli receptor FepA reveal residues involved in ligand binding and transport
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In silico Study of Toll-Like Receptor 4 Binding Site of FimH from Uropathogenic Escherichia coli
Introduction : The innate immune system as the first line of defense against the pathogens recognizes pathogen-associated molecular patterns (PAMPs) by Toll-Like Receptors (TLRs). Interaction of bacterial PAMPs by TLRs results in activation of innate and acquired immunity. FimH adhesin, a minor component of type 1 fimbriae encoded by Uropathogenic Escherichia coli (UPEC) is a PAMP of TLR4 tha...
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Bacterial resistance to mercury compounds (mercurials) is mediated by proteins encoded by mercury resistance (mer) operons. Six merE variants with site-directed mutations were constructed to investigate the roles of the cysteine and histidine residues in MerE protein during mercurial transport. By comparison of mercurial uptake by the cell with intact and/or variant MerE, we showed that the cys...
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Escherichin coli strain W is capable of actively transporting L-cystine as well as the structurally related compound OL,Ediaminopimelic acid. Cystine transport is mediated by two systems distinguishable on the basis of specificity and affinity for substrate. The cystine general system (K, = 3 x 10e7 M) also transports diaminopimelic acid and is inhibited by a variety of analogues, while the cys...
متن کاملAromatic 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 کاملConfined Mobility of TonB and FepA in Escherichia coli Membranes
The important process of nutrient uptake in Escherichia coli, in many cases, involves transit of the nutrient through a class of beta-barrel proteins in the outer membrane known as TonB-dependent transporters (TBDTs) and requires interaction with the inner membrane protein TonB. Here we have imaged the mobility of the ferric enterobactin transporter FepA and TonB by tracking them in the membran...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2001
ISSN: 0950-382X,1365-2958
DOI: 10.1046/j.1365-2958.2001.02473.x