5ZR2

Crystal Structure of Phosphoserine Phosphatase Mutant (H9A) from Entamoeba histolytica in complex with Phosphoserine

5ZR2 の概要

• エントリーDOI: 10.2210/pdb5zr2/pdb
• 分子名称: Phosphoglycerate mutase family protein, putative, PHOSPHOSERINE, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: histidine phosphatase superfamily, phosphoserine phosphatase, cysteine biosynthetic pathway, hydrolase
• 由来する生物種: Entamoeba histolytica HM-1:IMSS-A
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 96048.80

構造登録者

Kumari, P.,Gourinath, S. (登録日: 2018-04-23, 公開日: 2019-04-24, 最終更新日: 2023-11-22)

主引用文献

Kumari, P.,Babuta, M.,Bhattacharya, A.,Gourinath, S.
Structural and functional characterisation of phosphoserine phosphatase, that plays critical role in the oxidative stress response in the parasite Entamoeba histolytica.
J.Struct.Biol., 206:254-266, 2019

PubMed Abstract: Amoebiasis is a common parasitic infection in the developing world and is caused by the protist Entameoba histolytica. The proliferation of E. histolytica and its ability to invade epithelial tissues have been shown in several studies to be greatly decreased during oxidative stress. It is therefore not surprising that this amoeba has evolved several mechanisms to evade oxidative stress. Cysteine is thought to be one of the crucial molecules that help in redox defence, and a de novo cysteine biosynthetic pathway involving serine as one of the substrates has been partially elucidated in E. histolytica. Though most of the enzymes of this pathway in E. histolytica have been characterized, phosphoserine phosphatase (EhPSP), a key regulatory enzyme of the serine biosynthetic pathway, has not yet even been identified. In the current work, we identified and characterized EhPSP using various molecular, structural and functional approaches. The crystal structures of native and substrate-bound EhPSP were determined and showed the residues that play a crucial role in its phosphatase activity and substrate binding. Structural and biochemical studies indicated that EhPSP belongs to the histidine phosphatase superfamily. EhPSP-overexpressing amoebic cells were found to be more tolerant to oxidative stress. However, protection during oxidative stress was not seen when a functionally defective mutant was overexpressed. Our results clearly showed that E. histolytica has a functional PSP and that this protein participates in protecting the organism against oxidative stress.

PubMed: 30935984
DOI: 10.1016/j.jsb.2019.03.012

実験手法

X-RAY DIFFRACTION (2.95 Å)