A salt bridge of the C‐terminal carboxyl group regulates PHPT1 substrate affinity and catalytic activity
Erik Zavala,
Stephen Dansereau,
Michael J. Burke
et al.
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… Show more
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