6RCZ

The structure of Burkholderia pseudomallei trehalose-6-phosphatase

Summary for 6RCZ

• Entry DOI: 10.2210/pdb6rcz/pdb
• Descriptor: Trehalose 6-phosphate phosphatase, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: phosphatase, hydrolase
• Biological source: Burkholderia pseudomallei (strain K96243)
• Total number of polymer chains: 2
• Total formula weight: 57387.57

Authors

Gourlay, L.J. (deposition date: 2019-04-12, release date: 2020-02-19, Last modification date: 2024-05-15)

Primary citation

Suthisawat, S.,Gourlay, L.J.,Bolognesi, M.,Boonyuen, U.,Vanaporn, M.
Functional and structural analysis of trehalose-6-phosphate phosphatase from Burkholderia pseudomallei: Insights into the catalytic mechanism.
Biochem.Biophys.Res.Commun., 523:979-984, 2020

PubMed Abstract: We report the functional and structural characterization of trehalose-6-phosphate phosphatase (TPP), from the Gram-negative bacterium B. pseudomallei that causes melioidosis, a severe infectious disease endemic in Southeast Asia and Northern Australia. TPP is a key enzyme in the trehalose biosynthesis pathway, which plays an important role in bacterial stress responses. Due to the absence of this biosynthetic pathway in mammals, TPP has drawn attention as a potential drug target, to combat antibiotic resistance. In this context, we present a detailed biochemical analysis of purified recombinant TPP, reporting its specific high catalytic activity toward the trehalose-6-phosphate substrate, and an absolute requirement for its Mg cofactor. Furthermore, we present the crystal structure of TPP solved at 1.74 Å, revealing the canonical haloacid dehalogenase (HAD) superfamily fold and conserved substrate binding pocket, from which insights into the catalytic mechanism may be deduced. Our data represent a starting point for the rational design of antibacterial drugs.

PubMed: 31973820
DOI: 10.1016/j.bbrc.2019.12.088

Experimental method

X-RAY DIFFRACTION (1.74 Å)