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

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...

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Detalhes bibliográficos
Publicado no:J Biol Chem
Main Authors: 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.
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2020
Assuntos:
Membrane Biology
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC7152776/
https://ncbi.nlm.nih.gov/pubmed/32098871
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.RA119.011850
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