Structural characterization of regulatory proteins useful in developing biosensors for water purification systems

This thesis focuses on structural characterization of a bacterial protein, MopR, that is involved in direct sensing of toxic aromatic pollutants from the environment and hence, can provide a suitable scaffold for phenolic biosensor design. However, due to lack of any structural information till date, accurate biosensor design was impeded. Here, in this work, the first x-ray structure of the phenol sensing domain of MopR has been solved in complex with phenol derivatives which reveals the exact pollutant binding pocket architecture, which in turn, helped in designing a series of sensitive and selective biosensors for different phenolic pollutants accurately, by logic-based tweaking of the pocket.