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Article

The beta-barrel domain of FhuADelta5-160 is sufficient for TonB-dependent FhuA activities of Escherichia coli.

Molecular microbiology - 1 Sept 1999

Braun M, Killmann H, Braun V

Abstract excerpt

FhuA in the outer membrane of Escherichia coli serves as a transporter for ferrichrome, the antibiotics albomycin and rifamycin CGP4832, colicin M, and as receptor for phages T1, T5 and phi80. The previously determined crystal structure reveals that residues 160-714 of the mature protein form a beta-barrel that is closed from the periplasmic side by the globular N-proximal fragment, residues 1-159, designated the...

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Identifiers

PMID: 10476037
DOI: 10.1046/j.1365-2958.1999.01546.x

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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.

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The beta-barrel domain of FhuADelta5-160 is sufficient for TonB-dependent FhuA activities of Escherichia coli.PMID 10476037Read ↗

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

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In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12.Semantic proximity Read ↗

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

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

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

Transport of iron across the outer membrane.Semantic proximity Read ↗

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

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