What is it about?
The opportunistic bacterium Pseudomonas aeruginosa has been recognised as an important pathogen of clinical relevance and is a leading cause of hospital-acquired infections. The presence of a glycolytic enzyme in Pseudomonas that is known to be inhibited by trehalose 6-phosphate (T6P) in other organisms, suggests that these bacteria may be vulnerable to the detrimental effects of intra-cellular T6P accumulation. _x000D_ In the present study, we explored the structural and functional properties of trehalose 6-phosphate phosphatase (TPP) in P. aeruginosa in support of future target-based drug discovery. A survey of genomes revealed the existence of two TPP genes with either chromosomal or extra-chromosomal location. Both TPPs were produced as recombinant proteins and characterisation of their enzymatic properties confirmed specific, magnesium-dependent catalytic hydrolysis of trehalose 6-phosphate. The three-dimensional crystal structure of the chromosomal TPP revealed a protein dimer arising through β-sheet expansion of the individual monomers which possess the overall fold of halo-acid dehydrogenases.
The following have contributed to this page: Dr Andreas Hofmann and Associate Professor Mark J Coster