Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate

@article{Stuckey1994CrystalSO,
  title={Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 {\AA} and the complex with tungstate},
  author={Jeanne A. Stuckey and Heidi L. Schubert and Eric B. Fauman and Zhon-Yin Zhang and Jack E. Dixon and Mark A. Saper},
  journal={Nature},
  year={1994},
  volume={370},
  pages={571-575}
}
PROTEIN tyrosine phosphatases (PTPases) and kinases coregulate the critical levels of phosphorylation necessary for intracellular signalling, cell growth and differentiation1,2. Yersinia, the causative bacteria of the bubonic plague and other enteric diseases, secrete an active PTPase3, Yop51, that enters and suppresses host immune cells4,5. Though the catalytic domain is only ∼20% identical to human PTP1B6, the Yersinia PTPase contains all of the invariant residues present in eukaryotic… 
A ligand‐induced conformational change in the yersinia protein tyrosine phosphatase
TLDR
It is speculated that the intrinsic loop flexibility of different PTPases may be related to their catalytic rate and may play a role in the wide range of activities observed within this enzyme family.
The X-ray Crystal Structures of Yersinia Tyrosine Phosphatase with Bound Tungstate and Nitrate
TLDR
X-ray crystal structures of the Yersinia tyrosine phosphatase in complex with tungstate and nitrate have been solved to 2.4-Å resolution and are consistent with a general acid-catalyzed, in-line displacement of the phosphate moiety to Cys403 on the enzyme, followed by attack by a nucleophilic water molecule to release orthophosphate.
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.
Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution.
TLDR
The model presents a framework for understanding not only the classical Mn2+/Mg2+‐dependent protein phosphatases but also the sequence‐related domains of mitochondrial pyruvate dehydrogenase phosphatase, the Bacillus subtilusosphatase SpoIIE and a 300‐residue domain within yeast adenyl cyclase.
Crystal Structure of the Yersinia Protein-tyrosine Phosphatase YopH Complexed with a Specific Small Molecule Inhibitor*
TLDR
A specific YopH small molecule inhibitor is identified, p-nitrocatechol sulfate (pNCS), which exhibits a Ki value of 25 μm for Yop H and displays a 13–60-fold selectivity in favor of Yoph against a panel of mammalian PTPs.
Identification of Residues in the N-terminal Domain of theYersinia Tyrosine Phosphatase That Are Critical for Substrate Recognition*
TLDR
The random mutagenesis in combination with the yeast two-hybrid system indicated that the substrate- and SycH-binding activities of the YopH N-terminal domain can be separated and that the former activity is important for recognition and dephosphorylation of substrates by YOpHin vivo.
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.
Dynamics of the WPD loop of the Yersinia protein tyrosine phosphatase.
TLDR
Simulation results shed light on the role of the WPD loop in PTPase-mediated catalysis, and are useful in structure-based design for novel, selective YopH inhibitors as antibacterial drugs.
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