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

Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions.

Journal of bacteriology - 1 May 1997

Larsen R A, Foster-Hartnett D, McIntosh M A, Postle K

Abstract excerpt

The transport of Fe(III)-siderophore complexes and vitamin B12 across the outer membrane of Escherichia coli is an active transport process requiring a cognate outer membrane receptor, cytoplasmic membrane-derived proton motive force, and an energy-transducing protein anchored in the cytoplasmic membrane, TonB. This process requires direct physical contact between the outer membrane receptor and TonB. Previous...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Carrier Proteins
Share to Escherichia coli

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

Share to Escherichia coli Proteins

Share to Genes, Bacterial

Share to Membrane Proteins

Share to Mutation

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 9150216
DOI: 10.1128/jb.179.10.3213-3221.1997
PMCID: PMC179099

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

Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions.PMID 9150216Read ↗

Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA.Semantic proximity Read ↗

TonB interacts with nonreceptor proteins in the outer membrane of Escherichia coli.Semantic proximity Read ↗

Interactions between the outer membrane ferric citrate transporter FecA and TonB: studies of the FecA TonB box.Semantic proximity Read ↗

Partial suppression of an Escherichia coli TonB transmembrane domain mutation (delta V17) by a missense mutation in ExbB.Semantic proximity Read ↗

Mutations in the ExbB cytoplasmic carboxy terminus prevent energy-dependent interaction between the TonB and ExbD periplasmic domains.Semantic proximity Read ↗

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

Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli.Semantic proximity Read ↗

Sequence changes in the ton box region of BtuB affect its transport activities and interaction with TonB protein.Semantic proximity Read ↗

TonB and the gram-negative dilemma.Semantic proximity Read ↗

His(20) provides the sole functionally significant side chain in the essential TonB transmembrane domain.Semantic proximity Read ↗

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

Monomeric TonB and the Ton box are required for the formation of a high-affinity transporter-TonB complex.Semantic proximity Read ↗

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