Article
Specific in vivo thiol-labeling of the FhuA outer membrane ferrichrome transport protein of Escherichia coli K-12: evidence for a disulfide bridge in the predicted gating loop.
FEMS microbiology letters - 15 Aug 1997
Bös C, Braun V
Abstract excerpt
The multifunctional FhuA protein of Escherichia coli K-12 forms a channel that is closed by a loop, tentatively designated the 'gating loop', which is also the principal binding site for all FhuA ligands. In this report, it is shown by in vivo labeling that the two cysteines in the gating loop form a disulfide bridge, and they react weakly after reduction with biotin-maleimide, as determined by...
Topics
- Amino Acid Sequence
- Bacterial Outer Membrane Proteins
- Biotin
- Cysteine
- Disulfides
- Escherichia coli
- Escherichia coli Proteins
- Ferrichrome
- Hot Temperature
- Ligands
- Maleimides
- Molecular Sequence Data
- Mutation
- Oxidation-Reduction
- Protein Conformation
- Protein Denaturation
- Receptors, Virus
- Sulfhydryl Reagents