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Article

Exchangeability of N termini in the ligand-gated porins of Escherichia coli.

The Journal of biological chemistry - 20 Apr 2001

Scott D C, Cao Z, Qi Z, Bauler M, Igo J D, Newton S M, Klebba P E

Abstract excerpt

The ferric siderophore transporters of the Gram-negative bacterial outer membrane manifest a unique architecture: Their N termini fold into a globular domain that lodges within, and physically obstructs, a transmembrane porin beta-barrel formed by their C termini. We exchanged and deleted the N termini of two such siderophore receptors, FepA and FhuA, which recognize and transport ferric enterobactin and...

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Share to Ligands
Share to Bacterial Outer Membrane Proteins
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Share to Protein Structure, Secondary

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Source

Identifiers

PMID: 11278876
DOI: 10.1074/jbc.M011282200

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.

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Exchangeability of N termini in the ligand-gated porins of Escherichia coli.PMID 11278876Read ↗

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