Staphylococcus aureus, a prominent human pathogen, employs a specific enzyme to evade the immune system. This enzyme converts antimicrobial fatty acids in the cellular membrane into anti-inflammatory compounds that protect the pathogen against the host inflammatory response. Understanding the membrane-binding mechanism of this enzyme is essential for developing new strategies to combat S. aureus infections.

As highlighted in our recent publication in J. Biol. Chem., Resource researchers employed molecular dynamics simulations using NAMD to study this mechanism. Utilizing a specifically designed membrane model with enhanced lipid motion, they captured how the enzyme binds to the membrane and described its pose within the membrane. These findings provide molecular insights into S. aureus' virulence and highlight potential targets for novel therapeutic interventions.

Nearly 80% of the patients suffering from glycogen storage disease have a single mutation in their genome. The product of this gene mediates critical steps in sugar metabolism and storage. However, the molecular basis for the malfunction caused by this and similar mutations has remained unknown due to a lack of structural data. The advent of AlphaFold provided us with the first model of this important protein. As reported in a recent publication in PNAS Nexus, Resource researchers have produced large conformational ensembles of this protein in the empty and sugar-bound forms for both native and 10 clinically-relevant mutants. By identifying the structural and energetic effects of such mutations, using NAMD and VMD, we have begun to elucidate the role of each residue in the dysfunction of the enzyme.