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Crystal structure and putative substrate identification for the Entamoeba histolytica low molecular weight tyrosine phosphatase.

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.

journal_name

Mol Biochem Parasitol

journal_title

Molecular and biochemical parasitology

authors

Linford AS,Jiang NM,Edwards TE,Sherman NE,Van Voorhis WC,Stewart LJ,Myler PJ,Staker BL,Petri WA Jr

doi

10.1016/j.molbiopara.2014.01.003

subject

Has Abstract

pub_date

2014-01-01 00:00:00

pages

33-44

issue

1

eissn

0166-6851

issn

1872-9428

pii

S0166-6851(14)00013-9

journal_volume

193

pub_type

杂志文章

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