3JS5

Crystal structure of protein tyrosine phosphatase from Entamoeba histolytica with Hepes in the active site. High resolution, alternative crystal form with 1 molecule in asymmetric unit

3JS5 の概要

• エントリーDOI: 10.2210/pdb3js5/pdb
• 関連するPDBエントリー: 3IDO 3ILY
• 分子名称: Protein tyrosine phosphatase, SODIUM ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: niaid, ssgcid, seattle structural genomics center for infectious disease, parasitic protozoan, dysentery, phosphotyrosine, phosphatase, hydrolase
• 由来する生物種: Entamoeba histolytica
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20643.55

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2009-09-09, 公開日: 2009-09-22, 最終更新日: 2023-09-06)

主引用文献

Linford, A.S.,Jiang, N.M.,Edwards, T.E.,Sherman, N.E.,Van Voorhis, W.C.,Stewart, L.J.,Myler, P.J.,Staker, B.L.,Petri, W.A.
Crystal structure and putative substrate identification for the Entamoeba histolytica low molecular weight tyrosine phosphatase.
Mol.Biochem.Parasitol., 193:33-44, 2014

PubMed Abstract: Entamoeba histolytica is a eukaryotic intestinal parasite of humans, and is endemic in developing countries. We have characterized the E. histolytica putative low molecular weight protein tyrosine phosphatase (LMW-PTP). The structure for this amebic tyrosine phosphatase was solved, showing the ligand-induced conformational changes necessary for binding of substrate. In amebae, it was expressed at low but detectable levels as detected by immunoprecipitation followed by immunoblotting. A mutant LMW-PTP protein in which the catalytic cysteine in the active site was replaced with a serine lacked phosphatase activity, and was used to identify a number of trapped putative substrate proteins via mass spectrometry analysis. Seven of these putative substrate protein genes were cloned with an epitope tag and overexpressed in amebae. Five of these seven putative substrate proteins were demonstrated to interact specifically with the mutant LMW-PTP. This is the first biochemical study of a small tyrosine phosphatase in Entamoeba, and sets the stage for understanding its role in amebic biology and pathogenesis.

PubMed: 24548880
DOI: 10.1016/j.molbiopara.2014.01.003

実験手法

X-RAY DIFFRACTION (1.94 Å)