1a6q
From Proteopedia
|
CRYSTAL STRUCTURE OF THE PROTEIN SERINE/THREONINE PHOSPHATASE 2C AT 2 A RESOLUTION
Overview
Protein phosphatase 2C (PP2C) is a Mn2+- or Mg2+-dependent protein Ser/Thr, phosphatase that is essential for regulating cellular stress responses in, eukaryotes. The crystal structure of human PP2C reveals a novel protein, fold with a catalytic domain composed of a central beta-sandwich that, binds two manganese ions, which is surrounded by alpha-helices. Mn2+-bound, water molecules at the binuclear metal centre coordinate the phosphate, group of the substrate and provide a nucleophile and general acid in the, dephosphorylation reaction. Our model presents a framework for, understanding not only the classical Mn2+/Mg2+-dependent protein, phosphatases but also the sequence-related domains of mitochondrial, pyruvate dehydrogenase phosphatase, the Bacillus subtilus phosphatase, SpoIIE and a 300-residue domain within yeast adenyl cyclase. The protein, architecture and deduced catalytic mechanism are strikingly similar to the, PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C, shares no sequence similarity, suggestive of convergent evolution of, protein Ser/Thr phosphatases.
About this Structure
1A6Q is a Single protein structure of sequence from Homo sapiens with MN and PO4 as ligands. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution., Das AK, Helps NR, Cohen PT, Barford D, EMBO J. 1996 Dec 16;15(24):6798-809. PMID:9003755
Page seeded by OCA on Tue Dec 18 14:10:08 2007
