The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase

@article{Su1994TheCS,
  title={The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase},
  author={Xiao-Dong Su and Niccol{\`o} Taddei and Massimo Stefani and Giampietro Ramponi and P{\"a}r Nordlund},
  journal={Nature},
  year={1994},
  volume={370},
  pages={575-578}
}
PROTEIN tyrosine phosphorylation and dephosphorylation are central reactions for control of cellular division, differentiation and development1. Here we describe the crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase (PTPase)2, a cytosolic phosphatase present in many mammalian cells. The enzyme catalyses the dephosphorylation of phosphotyrosine-containing substrates3–6, and overexpression of the protein in normal and transformed cells inhibits cell proliferation7,8… 
Crystal Structure of a Human Low Molecular Weight Phosphotyrosyl Phosphatase
TLDR
The x-ray crystallographic structure of a human low molecular weight PTPase solved by molecular replacement to 2.2 Å is presented and possible aromatic residue interactions with the phosphotyrosine substrate are proposed from an examination of the binding site of the inhibitors.
Solution Structure of a Low-Molecular-Weight Protein Tyrosine Phosphatase from Bacillus subtilis
  • Huimin Xu, B. Xia, C. Jin
  • Chemistry
    Journal of bacteriology
  • 2006
TLDR
The solution structure of YwlE, an LMW PTP identified from the gram-positive bacteria Bacillus subtilis, is reported and the solution structure in combination with the backbone dynamics provides insights into the mechanism of substrate specificity of bacterial L MW PTPs.
Crystal Structure of Low-Molecular-Weight Protein Tyrosine Phosphatase from Mycobacterium tuberculosis at 1.9-Å Resolution
TLDR
The crystal structure of LMWPTPase of microbial origin, the first of its kind from Mycobacterium tuberculosis, is reported, and differences are observed in the residues involved, suggesting that they have a role in influencing different substrate specificities.
The Inactivation Mechanism of Low Molecular Weight Phosphotyrosine-protein Phosphatase by H2O2 *
TLDR
It is suggested that oxidative stress conditions and other processes producing hydrogen peroxide regulate the LMW-PTP in thecell, because a physiological concentration of H2O2 produces enzyme inactivation and considering that the activity is restored by reduction with low molecular weight thiols.
Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis.
  • Z. Zhang
  • Biology, Chemistry
    Critical reviews in biochemistry and molecular biology
  • 1998
TLDR
Biochemical experiments demonstrate that phosphatases in the PTPase superfamily utilize a common mechanism for catalysis going through a covalent thiophosphate intermediate that involves the nucleophilic Cys residue in thePTPase signature motif.
Crystal Structure of the Catalytic Domain of Protein-tyrosine Phosphatase SHP-1*
TLDR
Sequence alignment and structural analysis suggest that the residues in the WPD loop, especially the amino acid following Asp421, are critical for the movement of W PD loop on binding substrates and the specific activity of protein-tyrosine phosphatases.
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TLDR
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