comparison of LuxR and LasR The hyd

comparison of LuxR and LasR The hydrophobic active sites of LuxR and LasR both—individually as well as in superimposed state—are represented in Fig. 1. It was found that the active sites of both AHL receptors had similar structural traits that included a five-stranded antiparallel β-sheet packed against three α-helices on each side. The cavity was found to be formed by a cluster of hydrophobic and aromatic residues. Superimposition of both proteins also showed the ligand-binding cleft was identical and therefore, may have similar ligand-binding properties. This supports our hypothesis that if curcumin binds efficiently with LasR it may bind to LuxR with similar affinity, corroborating its anti-QS property. Pairwise sequence alignment of both the proteins showed only 20% similarity, still both the proteins possess high degree of structural similarity at the active site