In order to establish infection， pathogenic bacteria must obtain essential nutrients such as iron. Under acidic and/or anaerobic conditions， most bacteria utilize the Feo system in order to acquire ferrous iron (Fe ) from their host environment. The mechanism of this process， including its regulation， remains poorly understood. In this work， we have determined the crystal structure of FeoA from the nosocomial agent Klebsiella pneumoniae (KpFeoA). Our structure reveals an SH3-like domain that mediates interactions between neighboring polypeptides via hydrophobic intercalations into a Leu-rich surface ridge. Using docking of a small peptide corresponding to a postulated FeoB partner binding site， we demonstrate that KpFeoA can assume both "open" and "closed" conformations， controlled by binding at this Leu-rich ridge. We propose a model in which a "C-shaped" clamp along the FeoA surface mediates interactions with its partner protein， FeoB. These findings are the first to demonstrate atomic-level details of FeoA-based protein-protein interactions and provide a framework for testing FeoA-FeoB interactions， which could be exploited for future antibiotic developments.