Variations in the binding pocket of an inhibitor of the bacterial division protein FtsZ across genotypes and species.

ABSTRACT: The recent increase in antibiotic resistance in pathogenic bacteria calls for new approaches to drug-target selection and drug development. Targeting the mechanisms of action of proteins involved in bacterial cell division bypasses problems associated with increasingly ineffective variants of older antibiotics; to this end, the essential bacterial cytoskeletal protein FtsZ is a promising target. Recent work on its allosteric inhibitor, PC190723, revealed in vitro activity on Staphylococcus aureus FtsZ and in vivo antimicrobial activities. However, the mechanism of drug action and its effect on FtsZ in other bacterial species are unclear. Here, we examine the structural environment of the PC190723 binding pocket using PocketFEATURE, a statistical method that scores the similarity between pa

SUBMITTER: Miguel A 

PROVIDER: S-EPMC4374959 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature