NDLI: Double mutagenesis of a positive charge cluster in the ligand-binding site of the ferric enterobactin receptor, FepA

Content Provider	PubMed Central
Author	Newton, Salete M. C. Allen, Jennifer S. Cao, Zhenghua Qi, Zengbiao Jiang, Xunqing Cathy, Sprencel Igo, John D. Foster, Samuel B. Payne, Marvin A. Klebba, Phillip E.
Copyright Year	1997
Abstract	Siderophores and colicins enter bacterial cells through TonB-dependent outer membrane proteins. Using site-directed substitution mutagenesis, we studied ligand recognition by a prototypic Escherichia coli siderophore receptor, FepA, that binds the iron chelate ferric enterobactin and colicins B and D. These genetic experiments identified a common binding site for two of the three ligands, containing multiple positive charges, within cell surface residues of FepA. Elimination of single residues in this region did not impair the adsorption or transport of ferric enterobactin, but double mutagenesis in the charge cluster identified amino acids (Arg-286 and Arg-316) that participate in siderophore binding and function in FepA-mediated killing by colicins B and D. Ferric enterobactin binding, furthermore, prevented covalent modification of FepA within this domain by either a fluorescent probe or an arginine-specific reagent, corroborating the involvement of this site in ligand recognition. These results identify, for the first time, residues in a TonB-dependent outer membrane protein that participate in ligand binding. They also explain the competition between ferric enterobactin and the colicins on the bacterial cell surface: all three ligands interact with the same arginine residues within FepA during their penetration through the outer membrane.
Starting Page	4560
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	94
Language	English
Publisher	The National Academy of Sciences of the USA
Publisher Date	1997-04-29
Access Restriction	Open
Rights Holder	The National Academy of Sciences of the USA
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Double mutagenesis of a positive charge cluster in the ligand-binding site of the ferric enterobactin receptor, FepA.

Permeability properties of a large gated channel within the ferric enterobactin receptor, FepA.

Molecular analysis of the Escherichia coli ferric enterobactin receptor FepA.

Concerted loop motion triggers induced fit of FepA to ferric enterobactin

Direct Measurements of the Outer Membrane Stage of Ferric Enterobactin Transport POSTUPTAKE BINDING

Concerted loop motion triggers induced fit of FepA to ferric enterobactin

Identification of the second cluster of ligand-binding repeats in megalin as a site for receptor–ligand interactions

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

Evidence of Ball-and-chain Transport of Ferric Enterobactin through FepA*

Double mutagenesis of a positive charge cluster in the ligand-binding site of the ferric enterobactin receptor, FepA

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Double mutagenesis of a positive charge cluster in the ligand-binding site of the ferric enterobactin receptor, FepA.

Permeability properties of a large gated channel within the ferric enterobactin receptor, FepA.

Molecular analysis of the Escherichia coli ferric enterobactin receptor FepA.

Concerted loop motion triggers induced fit of FepA to ferric enterobactin

Direct Measurements of the Outer Membrane Stage of Ferric Enterobactin Transport POSTUPTAKE BINDING

Concerted loop motion triggers induced fit of FepA to ferric enterobactin

Identification of the second cluster of ligand-binding repeats in megalin as a site for receptor–ligand interactions

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Double mutagenesis of a positive charge cluster in the ligand-binding site of the ferric enterobactin receptor, FepA