4QXD

Crystal structure of Inositol Polyphosphate 1-Phosphatase from Entamoeba histolytica

「4J13」から置き換えられました

4QXD の概要

• エントリーDOI: 10.2210/pdb4qxd/pdb
• 分子名称: 3'(2'),5'-bisphosphate nucleotidase, putative, PHOSPHATE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: 1d-myo-inositol 1, 4-bisphosphate, hydrolysis, 1d-myo-inositol 4-phosphate, phosphate, hydrolase
• 由来する生物種: Entamoeba histolytica HM-1:IMSS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 66644.05

構造登録者

Tarique, K.F.,Abdul Rehman, S.A.,Betzel, C.,Gourinath, S. (登録日: 2014-07-19, 公開日: 2014-08-06, 最終更新日: 2024-04-03)

主引用文献

Tarique, K.F.,Abdul Rehman, S.A.,Betzel, C.,Gourinath, S.
Structure-based identification of inositol polyphosphate 1-phosphatase from Entamoeba histolytica
Acta Crystallogr.,Sect.D, 70:3023-3033, 2014

PubMed Abstract: Inositol polyphosphate 1-phosphatase from Entamoeba histolytica (EhIPPase) is an Mg(2+)-dependent and Li(+)-sensitive enzyme that catalyzes the hydrolysis of inositol 1,4-bisphosphate [Ins(1,4)P2] into myo-inositol 1-monophosphate and PO4(3-). In the present work, EhIPPase has been biochemically identified and its crystal structure has been determined in the presence of Mg(2+) and PO4(3-) at 2.5 Å resolution. This enzyme was previously classified as a 3'(2'),5'-bisphosphate nucleotidase in the NCBI, but its biochemical activity and structural analysis suggest that this enzyme behaves more like an inositol polyphosphate 1-phosphatase. The ability of EhIPPase to hydrolyze the smaller Ins(1,4)P2 better than the bulkier 3'-phosphoadenosine 5'-phosphate (PAP) is explained on the basis of the orientations of amino-acid residues in the binding site. This structure is the first of its class to be determined from any protozoan parasite, and is the third to determined among all organisms, following its rat and bovine homologues. The three-dimensional fold of EhIPPase is similar to those of other members of the inositol monophosphatase superfamily, which also includes inositol monophosphatase, 3'(2'),5'-bisphosphate nucleotidase and fructose-1,6-bisphosphate 1-phosphatase. They all share conserved residues essential for metal binding and substrate hydrolysis, with the motif D-Xn-EE-Xn-DP(I/L)DG(S/T)-Xn-WD-Xn-GG. The structure is divided into two domains, namely α+β and α/β, and the substrate and metal ions bind between them. However, the ability of each enzyme class to act specifically on its cognate substrate is governed by the class-specific amino-acid residues at the active site.

PubMed: 25372691
DOI: 10.1107/S1399004714021245

実験手法

X-RAY DIFFRACTION (2.55 Å)