1phr
From Proteopedia
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THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE
Overview
Protein tyrosine phosphorylation and dephosphorylation are central, reactions for control of cellular division, differentiation and, development. Here we describe the crystal structure of a, low-molecular-weight phosphotyrosine protein phosphatase (PTPase), a, cytosolic phosphatase present in many mammalian cells. The enzyme, catalyses the dephosphorylation of phosphotyrosine-containing substrates, and overexpression of the protein in normal and transformed cells inhibits, cell proliferation. The structure of the low-molecular-weight PTPase, reveals an alpha/beta protein containing a phosphate-binding loop motif at, the amino end of helix alpha 1. This motif includes the essential, active-site residues Cys 12 and Arg 18 and bears striking similarities to, the active-site motif recently described in the structure of human PTP1B., The structure of the low-molecular-weight PTPase supports a reaction, mechanism involving the conserved Cys 12 as an attacking nucleophile in an, in-line associative mechanism. The structure also suggests a catalytic, role for Asp 129 in the reaction cycle.
About this Structure
1PHR is a Single protein structure of sequence from Bos taurus with SO4 as ligand. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase., Su XD, Taddei N, Stefani M, Ramponi G, Nordlund P, Nature. 1994 Aug 18;370(6490):575-8. PMID:8052313
Page seeded by OCA on Tue Nov 20 23:49:39 2007
