6D3V

Chromosomal trehalose-6-phosphate phosphatase from P. aeruginosa

Summary for 6D3V

• Entry DOI: 10.2210/pdb6d3v/pdb
• Related: 6cj0
• Descriptor: Trehalose phosphatase, ACETIC ACID, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: had superfamily/rossmann fold, trehalose-6-phosphate, phosphohydrolase, hydrolase, lyase
• Biological source: Pseudomonas sp. HMSC75E02
• Total number of polymer chains: 2
• Total formula weight: 56676.44

Authors

Hofmann, A.,Cross, M.,Park, S.-Y. (deposition date: 2018-04-17, release date: 2018-05-09, Last modification date: 2023-10-04)

Primary citation

Cross, M.,Biberacher, S.,Park, S.Y.,Rajan, S.,Korhonen, P.,Gasser, R.B.,Kim, J.S.,Coster, M.J.,Hofmann, A.
Trehalose 6-phosphate phosphatases of Pseudomonas aeruginosa.
FASEB J., 32:5470-5482, 2018

PubMed Abstract: The opportunistic bacterium Pseudomonas aeruginosa has been recognized as an important pathogen of clinical relevance and is a leading cause of hospital-acquired infections. The presence of a glycolytic enzyme in Pseudomonas, which 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 intracellular T6P accumulation. 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 2 TPP genes with either chromosomal or extrachromosomal location. Both TPPs were produced as recombinant proteins, and characterization of their enzymatic properties confirmed specific, magnesium-dependent catalytic hydrolysis of T6P. The 3-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.-Cross, M., Biberacher, S., Park, S.-Y., Rajan, S., Korhonen, P., Gasser, R. B., Kim, J.-S., Coster, M. J., Hofmann, A. Trehalose 6-phosphate phosphatases of Pseudomonas aeruginosa.

PubMed: 29688811
DOI: 10.1096/fj.201800500R

Experimental method

X-RAY DIFFRACTION (1.8 Å)