The siderophore enterobactin (Ent) is produced by many species of enteric bacteria to mediate iron uptake. This iron scavenger can be reincorporated by the bacteria as the ferric complex [Fe(III)(Ent)](3)(-) and is subsequently hydrolyzed by an esterase to facilitate intracellular iron release. Recent literature reports on altered protein recognition and binding of modified enterobactin increase the significance of understanding the structural features and solution chemistry of ferric enterobactin. Here we report the crystal structure of Ferric enterobactin esterase (Fes) from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2. The results provide a structural framework for understanding structural features of iron enterobactin regulation.
Transport and binding proteins; subcategory: Cations and iron carrying compounds