ArticleBiochemistry2012
New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
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- Conformational Dynamics and Catalytic Backups in a Hyper-thermostable Engineered Archaeal Protein Tyrosine Phosphatase.JACS Au · 2026Article
- Structural analysis of dual specificity phosphatases, the only type of protein tyrosine phosphatases found in humans and across diverse microorganisms.Journal of microbiology (Seoul, Korea) · 2025Review
- Significant Loop Motions in the SsoPTP Protein Tyrosine Phosphatase Allow for Dual General Acid Functionality.Biochemistry · 2021Article
- Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases.International journal of molecular sciences · 2020Article
- Allosteric Impact of the Variable Insert Loop inBiochemistry · 2020Article
- Synthesis and evaluation of novel purple acid phosphatase inhibitors.MedChemComm · 2019Article
- Kinetic isotope effects in the characterization of catalysis by protein tyrosine phosphatases.Biochimica et biophysica acta · 2015Review
- Article
- New functional aspects of the atypical protein tyrosine phosphatase VHZ.Biochemistry · 2013Article
- Specificity profiling of protein phosphatases toward phosphoseryl and phosphothreonyl peptides.Journal of the American Chemical Society · 2013Article
- Ligand binding reduces conformational flexibility in the active site of tyrosine phosphatase related to biofilm formation A (TpbA) from Pseudomonasaeruginosa.Journal of molecular biology · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The recently discovered 150-residue human VHZ (VH1-related protein, Z member) is one of the smallest protein tyrosine phosphatases (PTPs) known and contains only the minimal structural elements common to all PTPs. We report a substrate screening analysis and a crystal structure of the VHZ complex with vanadate at 1.1 Å resolution, with a detailed structural comparison with other members of the protein tyrosine phosphatase family, including classical tyrosine-specific protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DSPs). A screen with 360 phosphorylated peptides shows VHZ efficiently catalyzes the hydrolysis of phosphotyrosine (pY)-containing peptides but exhibits no activity toward phosphoserine (pS) or phosphothreonine (pT) peptides. The new structure reveals a deep and narrow active site more typical of the classical tyrosine-specific PTPs. Despite the high degrees of structural and sequence similarity between VHZ and classical PTPs, its general acid IPD-loop is most likely conformationally rigid, in contrast to the flexible WPD counterpart of classical PTPs. VHZ also lacks substrate recognition domains and other domains typically found on classical PTPs. It is therefore proposed that VHZ is more properly classified as an atypical PTP rather than an atypical DSP, as has been suggested.
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