Hinge-bending in L-arabinose-binding protein. The "Venus's-flytrap" model.
Theoretical conformational energy calculations show that large changes in the width of the binding-site cleft in the L-arabinose-binding protein involve only modest changes in the protein internal energy. Solvation energy changes associated with such variations of the cleft width and with protein-ligand interactions are estimated to be significantly larger than the internal energy changes. These results indicate that the binding-site cleft is open in the unliganded protein and is induced to close upon ligation. This picture is consistent with experimental data on the structure and binding kinetics of the L-arabinose-binding protein and provides a physical framework for interpreting such data.
D001426:Bacterial Proteins; D001665:Binding Sites; D002352:Carrier Proteins; D004926:Escherichia coli / Q000032:analysis; D029968:Escherichia coli Proteins; D008958:Models, Molecular; D011487:Protein Conformation
C016242:AraF protein, E coli; D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins