| Peptide deformylase (PDF) is a metalloproteinase and executes an essential step in the maturation of proteins in eubacteria, by removing the formyl group from the N-terminal methionine residue of ribosome-synthesized polypeptides. This process is crucial for bacterial survival because mature proteins do not retain N-formyl-methionine, and all known N-terminal peptidases cannot utilize formylated peptides as substrate. Thus, inhibition of PDF is essential to obstruct the bacterial protein maturation process. Antibiotics based on PDF inhibition have the potential to provide the much needed antibacterial activity against most of the major drug-resistant pathogens. This study comprises an implementation of _in-silico_ techniques to validate and map the... |
