Staphylococcus aureus is a Gram-positive bacterial pathogen, notorious for its ability to evolve resistance mechanisms against novel antibiotics. The ever-increasing prevalence of this superbug highlights the urgency to characterise novel drug targets against this pathogen. The enzymes involved in the degradation of sialic acids are promising targets, yet to be exploited. Sialic acids are found at the terminus of glycan molecules attached to the surface of eukaryotic cells. Interestingly, several bacterial pathogens scavenge sialic acid from their surrounding environment and degrade it as a source of carbon, nitrogen and energy. This sequestration and subsequent degradation of sialic acid requires a cluster of genes known as the ‘Nan-Nag’ cluster. This cluster encodes a sialic acid transporter and five catabolic enzymes (a lyase, kinase, wpimerase, deacetylase and deaminase) that successively degrade it. Importantly, this pathway has proven to be necessary for the colonisation and persistence of S. aureus, making it a viable target for drug design against this pathogen. A biophysical and structural characterisation of this pathway will be presented. Data obtained from analytical ultracentrifugation, small-angle X-ray scattering and X-ray crystallography will be included. Understanding the structural nature of these enzymes will provide us with the preliminary information necessary for antibiotic development.