Research Projects

CytR, a transcription regulator, plays a crucial role in E. coli's energy metabolism, particularly under stressed conditions. It regulates gene expression, maltose utilization, and heat-shock response. CytR's multi-functionality is due to its interaction with multiple promoter regions, including the uniquely disordered DNA binding domain (DBD). However, little is known about CytR's structural-mechanistic features, such as the cytidine binding signal and its binding affinity. The binding affinity is significant between two sub-domains of the LBD, suggesting a pre-equilibrium between open and closed conformations. Mutations can be engineered into CytR LBD to alter binding affinity.