6QJ6

The structure of Trehalose-6-phosphatase from Burkholderia pseudomallei

6QJ6 の概要

• エントリーDOI: 10.2210/pdb6qj6/pdb
• 分子名称: Trehalose 6-phosphate phosphatase, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: trehalose-6-phosphatase, hydrolase
• 由来する生物種: Burkholderia pseudomallei (strain K96243)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 57387.57

構造登録者

Gourlay, L.J. (登録日: 2019-01-23, 公開日: 2020-01-15, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.74 Å)