Bacteria utilise a suit of transcription factors to respond to a range of stimuli, be it changes in nutrient availability, host cell infection or the presence of antibiotics. One key set of bacterial transcription factors are the multi-antibiotic resistance regulator proteins (MarR proteins) which regulate gene products associated with antibiotic resistance mechanisms. While emphasis has been placed on the function of these proteins and uncovering which operons they regulate, less research has focused on understanding the molecular mechanisms that influence the recruitment or dissociation of these transcription factors. Previous research has shown that E. coli MarR forms disulphide mediated tetramers [1] which suggests a possible mechanism of regulation whereby an influx of cellular copper or the presence of antibiotics causes the oligomerisation of MarR and thus changes its ability to bind to DNA. However, whether this mechanism is conserved across other MarR homologues is unknown. To this end, we present the structural and biophysical characterisation of a MarR homologue from Klebsiella pneumoniae ; KvrA, that has been tied capsule formation in both hyper virulent and classical K. pneumoniae strains [2]. Ongoing work aims to structurally and functionally characterise KvrA in its dimeric and tetrameric form to determine potential oligomeric and conformational changes that may serve as KvrA regulatory mechanisms and identify potential KvrA binding sequences in Klebsiella. This work not only broadens our understanding of the mechanisms of transcriptional regulation but, given the MarR proteins’ involvement in resistance mechanisms, may offer a novel avenue for antibiotic development.