Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mutations in the Escherichia coli receptor FepA reveal residues involved in ligand binding and transport.

Molecular microbiology - 1 Aug 2001

Barnard T J, Watson M E, McIntosh M A

Abstract excerpt

FepA is the Escherichia coli outer membrane receptor for ferric enterobactin, colicin D and colicin B. The transport processes through FepA are energy-dependent, relying on the periplasmic protein TonB to interact with FepA. Through this interaction, TonB tranduces energy derived from the cytoplasmic membrane across the periplasmic space to FepA. In this study, random mutagenesis strategies were used to define...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Motifs
Share to Bacterial Outer Membrane Proteins
Share to Binding, Competitive

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Colicins

Share to Conserved Sequence

Share to Ligands

Share to Protein Transport

Share to Receptors, Cell Surface

Source

Identifiers

PMID: 11532122
DOI: 10.1046/j.1365-2958.2001.02473.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations in the Escherichia coli receptor FepA reveal residues involved in ligand binding and transport.PMID 11532122Read ↗

Molecular analysis of the Escherichia coli ferric enterobactin receptor FepA.Semantic proximity Read ↗

Identification and mutational studies of conserved amino acids in the outer membrane receptor protein, FepA, which affect transport but not binding of ferric-enterobactin in Escherichia coli.Semantic proximity Read ↗

Defined inactive FecA derivatives mutated in functional domains of the outer membrane transport and signaling protein of Escherichia coli K-12.Semantic proximity Read ↗

Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions.Semantic proximity Read ↗

Conformational rearrangements in the N-domain of Escherichia coli FepA during ferric enterobactin transport.Semantic proximity Read ↗

Surface topology of the Escherichia coli K-12 ferric enterobactin receptor.Semantic proximity Read ↗

Ferric hydroxamate binding protein FhuD from Escherichia coli: mutants in conserved and non-conserved regions.Semantic proximity Read ↗

Sequence of the fhuE outer-membrane receptor gene of Escherichia coli K12 and properties of mutants.Semantic proximity Read ↗

Insertion mutagenesis of the gene encoding the ferrichrome-iron receptor of Escherichia coli K-12.Semantic proximity Read ↗

A new glimpse of FadR-DNA crosstalk revealed by deep dissection of the E. coli FadR regulatory protein.Semantic proximity Read ↗

Loss of the Ferripyochelin Receptor FptA Drives Reduced Cefiderocol Susceptibility and Impairs Fitness in <i>Pseudomonas aeruginosa</i> PA14Semantic proximity Read ↗

Genetic insertion and exposure of a reporter epitope in the ferrichrome-iron receptor of Escherichia coli K-12.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.