The 1.35 Å resolution structure of the phosphatase domain of the suppressor of T-cell receptor signaling protein in complex with sulfate

The crystal structure of the phosphatase domain of Sts-1 at pH 4.6 complexed with sulfate has been determined to 1.35 Å resolution. The suppressor of T-cell signaling (Sts) proteins are multidomain proteins that negatively regulate the signaling of membrane-bound receptors, including the T-cell receptor (TCR) and the epidermal growth-factor receptor (EGFR). They contain at their C-terminus a 2H-phosphatase homology (PGM) domain that is responsible for their protein tyrosine phosphatase activity. Here, the crystal structure of the phosphatase domain of Sts-1, Sts-1_PGM, was determined at pH 4.6. The asymmetric unit contains two independent molecules and each active site is occupied by a sulfate ion. Each sulfate is located at the phosphate-binding site and makes similar interactions with the catalytic residues. The structure suggests an explanation for the lower Michaelis–Menten constants at acidic pH