ArticleProtein science : a publication of the Protein Society2024
A salt bridge of the C-terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity.
Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Inhibition of PHPT1 by phenylarsonic acids.Dalton transactions (Cambridge, England : 2003) · 2026Article
- PHPT1 acts as an inhibitor in high-altitude pulmonary hypertension via negative TRPV5 signaling regulation.Journal of translational medicine · 2025Article
- A Geranylated Natural Product Simamycin Disrupts the Allosteric Catalysis of tRNA-2-selenouridine Synthase SelU.Biochemistry · 2025Article
- A salt bridge of the C-terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity.Protein science : a publication of the Protein Society · 2024Article
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7 authors.
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Abstract
PHPT1 is a histidine phosphatase that modulates signaling in eukaryotes through its catalytic activity. Here, we present an analysis of the structure and dynamics of PHPT1 through a combination of solution NMR, molecular dynamics, and biochemical experiments. We identify a salt bridge formed between the R78 guanidinium moiety and the C-terminal carboxyl group on Y125 that is critical for ligand binding. Disruption of the salt bridge by appending a glycine residue at the C-terminus (G126) leads to a decrease in catalytic activity and binding affinity for the pseudo substrate, para-nitrophenylphosphate (pNPP), as well as the active site inhibitor, phenylphosphonic acid (PPA). We show through NMR chemical shift,
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