3JVI
Product state mimic crystal structure of protein tyrosine phosphatase from Entamoeba histolytica
Summary for 3JVI
| Entry DOI | 10.2210/pdb3jvi/pdb |
| Related | 3ILY 3JS5 |
| Descriptor | Protein tyrosine phosphatase, SULFATE ION (3 entities in total) |
| Functional Keywords | niaid, ssgcid, seattle structural genomics center for infectious disease, parasitic protozoan, dysentery, liver abscess, hydrolase |
| Biological source | Entamoeba histolytica |
| Total number of polymer chains | 1 |
| Total formula weight | 18487.09 |
| Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2009-09-16, release date: 2009-09-22, Last modification date: 2023-09-06) |
| Primary citation | 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 Cited by 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: 24548880DOI: 10.1016/j.molbiopara.2014.01.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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