Article
Maltose-binding protein containing an interdomain disulfide bridge confers a dominant-negative phenotype for transport and chemotaxis.
The Journal of biological chemistry - 26 Jul 1996
Zhang Y, Mannering D E, Davidson A L, Yao N, Manson M D
Abstract excerpt
Bacterial substrate-binding proteins exist in an equilibrium among four forms: open/substrate-free, open/substrate-bound, closed/substrate-free, and closed/substrate-bound. Ligands stabilize the closed conformation, whereas the open conformation predominates in the substrate-free species. In its...
Topics
- ATP-Binding Cassette Transporters
- Bacterial Proteins
- Biological Transport
- Carrier Proteins
- Chemotaxis
- Cysteine
- Disulfides
- Escherichia coli
- Escherichia coli Proteins
- Maltose
- Maltose-Binding Proteins
- Monosaccharide Transport Proteins
- Phenotype
- Protein Conformation