COMPUTATIONAL MODELING AND STRUCTURAL STUDIES OF THE UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE-2,6-DIAMINOPIMELATE LIGASE PROTEIN FROM PSEUDOMONAS AERUGINOSA

Abstract

The hospital relevance of Pseudomonas aeruginosa is considerable, therefore, studies should be conducted on proteins present in the bacterium that serve as therapeutic targets for the discovery of new antimicrobial drugs. Thus, enzymes such as UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-2,6-diaminopimelate ligase (MurE), which play an important metabolic role and are not homologous in mammals, represent valuable potential targets for the development of new drugs (AMERA et al., 2019). MurE participates in the synthesis of murein, a substance involved in the formation of the bacterial cell wall, an indispensable component for the microorganism’s survival. In this study, computational homology modeling was performed using the bioinformatics programs Modeller and T-Coffee. It is expected that these theoretical findings may be integrated with biochemical knowledge so that, in a future study, they may assist in the identification of ligands for MurE as a therapeutic target.