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Article

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

The Journal of biological chemistry - 10 Apr 2020

Majumdar Aritri, Trinh Vy, Moore Kyle J, Smallwood Chuck R, Kumar Ashish, Yang Taihao, Scott Daniel C, Long Noah J, Newton Salete M, Klebba Phillip E

Abstract excerpt

The Escherichia coli outer membrane receptor FepA transports ferric enterobactin (FeEnt) by an energy- and TonB-dependent, but otherwise a mechanistically undetermined process involving its internal 150-residue N-terminal globular domain (N-domain). We genetically introduced pairs of Cys residues in different regions of the FepA tertiary structure, with the potential to form disulfide bonds. These included Cys...

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Identifiers

PMID: 32098871
DOI: 10.1074/jbc.RA119.011850
PMCID: PMC7152776

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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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