Article
A Pro to Gly mutation in the hinge of the arabinose-binding protein enhances binding and alters specificity. Sugar-binding and crystallographic studies.
The Journal of biological chemistry - 25 Sept 1990
Vermersch P S, Tesmer J J, Lemon D D, Quiocho F A
Abstract excerpt
The L-arabinose-binding protein (ABP) of Escherichia coli consists structurally of two distinct globular domains connected by a hinge of three separate peptide segments. Arabinose is bound and completely sequestered within the deep cleft between the two domains. With reduced affinity, ABP also binds D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction). Experiments have been...
Topics
- Amino Acid Sequence
- Arabinose
- Base Sequence
- Binding Sites
- Carrier Proteins
- Computer Graphics
- Escherichia coli
- Escherichia coli Proteins
- Genes, Bacterial
- Glycine
- Kinetics