Pseudomonas aeruginosa is a gram-negative bacterium that can cause a wide range of serious infections that are challenging to treat via traditional methods [1]. Like many organisms P. aeruginosa has evolved complex systems to preserve internal zinc homeostasis allowing for the maintenance of optimal levels of this life-sustaining, but potentially toxic, micronutrient [1,2]. For pathogenic bacteria these systems are critical to their ability to effectively colonise eukaryotic hosts as they assist in overcoming host immune responses which sequester Zn2+ to slow pathogen growth [3]. Even amongst pathogenic bacteria P. aeruginosa is notably adept at thriving in zinc deficient environments which has been attributed to the presence of several high affinity zinc import systems in addition to the well characterised ZnuABC system found in most gram-negative bacteria [4]. These additional systems have been found to contribute significantly to P. aeruginosa’s extreme virulence making discovering how these systems function a focus of research efforts aiming to build a comprehensive model of how P. aeruginosa infects hosts [5].
One of these additional systems is the putative ABC transporter PA4063-66, which has been found to be the system with the highest expression in low zinc environments [6]. Unlike a typical ABC transporter the PA4063-66 system has two potential substrate binding proteins (SBPs), PA4063 and PA4066, which, despite both having a nanomolar affinity to zinc and being localised to the periplasm, lack typical SBP structures [4,5]. We have shown that these two proteins form a complex with a micromolar affinity, however, the addition of excess zinc causes complex dissociation suggesting that the binding of Zn2+ to one or both proteins destabilizes the complex structure. This poster will present our work on characterising the relationship between zinc binding and complex dissociation, in addition to the possible consequences of our results for mechanisms of Zn2+ homeostasis in P. aeruginosa.