3MBK

The 1.35 A Structure of the Phosphatase Domain of the Suppressor of T Cell Receptor Signalling Protein in Complex with Sulphate

Summary for 3MBK

• Entry DOI: 10.2210/pdb3mbk/pdb
• Related: 2H0Q
• Descriptor: Ubiquitin-associated and SH3 domain-containing protein B, SULFATE ION (3 entities in total)
• Functional Keywords: pgm, sts-1, signaling protein, low ph, nucleus, phosphoprotein, sh3 domain
• Biological source: Mus musculus (mouse)
• Cellular location: Cytoplasm : Q8BGG7
• Total number of polymer chains: 2
• Total formula weight: 59582.25

Authors

Nassar, N.,Jakoncic, J. (deposition date: 2010-03-25, release date: 2010-06-23, Last modification date: 2023-09-06)

Primary citation

Jakoncic, J.,Sondgeroth, B.,Carpino, N.,Nassar, N.
The 1.35 A resolution structure of the phosphatase domain of the suppressor of T-cell receptor signaling protein in complex with sulfate.
Acta Crystallogr.,Sect.F, 66:643-647, 2010

PubMed Abstract: 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.

PubMed: 20516590
DOI: 10.1107/S1744309110014259

Experimental method

X-RAY DIFFRACTION (1.35 Å)