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...
Topics
- Bacterial Outer Membrane Proteins
- Biological Transport
- Carrier Proteins
- Enterobactin
- Escherichia coli
- Models, Molecular
- Mutagenesis, Site-Directed
- Mutation
- Protein Binding
- Protein Conformation
- Protein Domains
- Receptors, Cell Surface