The harshness of
legionellosis differs from mild
Pontiac fever to potentially fatal
Legionnaire's disease. The increasing development of drug resistance against
legionellosis has led to explore new novel
drug targets. It has been found that
phosphoglucosamine mutase,
phosphomannomutase, and
phosphoglyceromutase enzymes can be used as the most probable therapeutic
drug targets through extensive data mining.
Phosphoglucosamine mutase is involved in
amino sugar and
nucleotide sugar metabolism. The purpose of this study was to predict the potential target of that specific
drug. For this, the 3D structure of
phosphoglucosamine mutase of Legionella pneumophila (strain Paris) was determined by means of homology modeling through Phyre2 and refined by ModRefiner. Then, the designed model was evaluated with a structure validation program, for instance, PROCHECK, ERRAT, Verify3D, and QMEAN, for further structural analysis. Secondary structural features were determined through self-optimized prediction method with alignment (SOPMA) and interacting networks by STRING. Consequently, we performed molecular docking studies. The analytical result of PROCHECK showed that 95.0% of the residues are in the most favored region, 4.50% are in the additional allowed region and 0.50% are in the generously allowed region of the Ramachandran plot. Verify3D graph value indicates a score of 0.71 and 89.791, 1.11 for ERRAT and QMEAN respectively. Arg419, Thr414, Ser412, and Thr9 were found to dock the substrate for the most favorable binding of S-mercaptocysteine. However, these findings from this current study will pave the way for further extensive investigation of this
enzyme in wet lab experiments and in that way assist
drug design against
legionellosis.