Trehalose 6-phosphate phosphatases of Pseudomonas aeruginosa

  • Megan Cross, Sonja Biberacher, Suk-Youl Park, Siji Rajan, Pasi Korhonen, Robin B. Gasser, Jeong-Sun Kim, Mark J. Coster, Andreas Hofmann
  • The FASEB Journal, October 2018, Federation of American Societies For Experimental Biology (FASEB)
  • DOI: 10.1096/fj.201800500r

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.

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The following have contributed to this page: Dr Andreas Hofmann and Associate Professor Mark J Coster