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Our group uses the technique of X-ray crystallography, as well as other biochemical approaches, to decipher the structure and function of enzymes involved in peptidoglycan synthesis in bacteria. Primarily, we study penicillin-binding proteins (PBPs), the well-known molecular targets for ß-lactam antibiotics. Mutations in these proteins are a major contributor to antibiotic resistance in bacteria and our current focus is to understand how such mutations impact the structure and kinetics of PBPs, with the goal of developing new antimicrobials that circumvent such mechanisms. Following our development of a fluorescence-polarization assay, we also conduct high-throughput screening against large chemical libraries to identify new inhibitors of PBPs for drug development. Finally, as X-ray crystallographers, we collaborate with a number of groups, both within MUSC and beyond, on various structural biology projects.
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