v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | This entry defines the ligand-binding and dimerisation domain of the bacterial regulatory protein AraC and other HTH-type transcriptional regulators. The crystal structure of the arabinose-binding and dimerisation domain of the Escherichia coli gene regulatory protein AraC was determined in the presence and absence of L-arabinose. The arabinose-bound molecule shows that the protein adopts an unusual fold, binding sugar within a beta barrel and completely burying the arabinose with the amino-terminal arm of the protein. Dimer contacts in the presence of arabinose are mediated by an antiparallel coiled-coil. In the uncomplexed protein, the amino-terminal arm is disordered, uncovering the sugar-binding pocket and allowing it to serve as an oligomerization interface []. |
| Short Name | AraC-bd |