1PHR

THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE

Summary for 1PHR

• Entry DOI: 10.2210/pdb1phr/pdb
• Descriptor: LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE, SULFATE ION (3 entities in total)
• Functional Keywords: phosphotyrosine protein phosphatase
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm: P11064
• Total number of polymer chains: 1
• Total formula weight: 18042.39

Authors

Su, X.-D.,Taddei, N.,Stefani, M.,Ramponi, G.,Nordlund, P. (deposition date: 1994-07-05, release date: 1995-07-31, Last modification date: 2024-02-14)

Primary citation

Su, X.D.,Taddei, N.,Stefani, M.,Ramponi, G.,Nordlund, P.
The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase.
Nature, 370:575-578, 1994

PubMed Abstract: Protein tyrosine phosphorylation and dephosphorylation are central reactions for control of cellular division, differentiation and development. Here we describe the crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase (PTPase), a cytosolic phosphatase present in many mammalian cells. The enzyme catalyses the dephosphorylation of phosphotyrosine-containing substrates, and overexpression of the protein in normal and transformed cells inhibits cell proliferation. The structure of the low-molecular-weight PTPase reveals an alpha/beta protein containing a phosphate-binding loop motif at the amino end of helix alpha 1. This motif includes the essential active-site residues Cys 12 and Arg 18 and bears striking similarities to the active-site motif recently described in the structure of human PTP1B. The structure of the low-molecular-weight PTPase supports a reaction mechanism involving the conserved Cys 12 as an attacking nucleophile in an in-line associative mechanism. The structure also suggests a catalytic role for Asp 129 in the reaction cycle.

PubMed: 8052313
DOI: 10.1038/370575a0

Experimental method

X-RAY DIFFRACTION (2.1 Å)