Gastric adenocarcinoma is the fifth most deadly cancer in the world. Over 90% of these cases are related to infection of Helicobacter pylori (H. pylori), a gastrointestinal pathogen present in over 50% of the population. Our collaborators at UTS (Associate Professor Iain Duggin) have demonstrated that a H.pylori dynamin knock-out is unable to survive acidic environments, suggesting that dynamins play an essential role in normal growth. We present bioinformatics results, including an Alphafold analysis and traditional sequence comparisons with the dynamin superfamily, which suggest these proteins, encoded in an operon pair, are likely to directly interact. We have overexpressed and purified both proteins to establish crystal screening trials for X-ray crystallography structural determination and have initiated biophysical experiments to analyse their interaction with each other, the cell membrane and their enzymatic features. We present some preliminary lipid-binding assays, cryo-EM imaging and mass photometry results. Finally, our current data taken in context with existing models for dynamin function enable a possible model for how these dynamin pairs may interact in vivo.