ArticleNature communications2022
A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Review
- Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates.FEBS letters · 2026Review
- Protein pyrophosphorylation by inositol pyrophosphates - detection, function, and regulation.FEBS letters · 2026Review
- Bridging Manual and Computational Approaches: The Pseudophosphatase Scanner for Genome-Wide Fungal Pseudophosphatome Analysis.ACS omega · 2026Article
- Loop dynamics, allostery, and function in protein tyrosine phosphatases: insights from molecular simulations.Biochemical Society transactions · 2026Review
- NUDIX hydrolases target specific inositol pyrophosphates and regulate phosphate homeostasis and bacterial pathogen susceptibility in Arabidopsis.Journal of integrative plant biology · 2025Article
- TENT5C functions as a corepressor in the ligand-bound glucocorticoid receptor and estrogen receptor α complexes.The FEBS journal · 2025Article
- Astragaloside IV alleviates septic myocardial injury through DUSP1-Prohibitin 2 mediated mitochondrial quality control and ER-autophagy.Journal of advanced research · 2025Article
- Visualizing and Identifying Inositol Pyrophosphate Isomers in Crystallo.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Inositol pyrophosphate catabolism by three families of phosphatases regulates plant growth and development.PLoS genetics · 2024Article
- Catalytic Redundancies and Conformational Plasticity Drives Selectivity and Promiscuity in Quorum Quenching Lactonases.JACS Au · 2024Article
- A deep intronic splice-alteringScience translational medicine · 2024Article
- Substrate promiscuity of inositol 1,4,5-trisphosphate kinase driven by structurally-modified ligands and active site plasticity.Nature communications · 2024Article
- Protein pyrophosphorylation by inositol phosphates: a novel post-translational modification in plants?Frontiers in plant science · 2024Review
- Loop dynamics and the evolution of enzyme activity.Nature reviews. Chemistry · 2023Review
- Article
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8 authors.
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Abstract
Structural snapshots of protein/ligand complexes are a prerequisite for gaining atomic level insight into enzymatic reaction mechanisms. An important group of enzymes has been deprived of this analytical privilege: members of the protein tyrosine phosphatase (PTP) superfamily with catalytic WPD-loops lacking the indispensable general-acid/base within a tryptophan-proline-aspartate/glutamate context. Here, we provide the ligand/enzyme crystal complexes for one such PTP outlier: Arabidopsis thaliana Plant and Fungi Atypical Dual Specificity Phosphatase 1 (AtPFA-DSP1), herein unveiled as a regioselective and efficient phosphatase towards inositol pyrophosphate (PP-InsP) signaling molecules. Although the WPD loop is missing its canonical tripeptide motif, this structural element contributes to catalysis by assisting PP-InsP delivery into the catalytic pocket, for a choreographed exchange with phosphate reaction product. Subsequently, an intramolecular proton donation by PP-InsP substrate is posited to substitute functionally for the absent aspartate/glutamate general-acid. Overall, we expand mechanistic insight into adaptability of the conserved PTP structural elements.
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