1a6q
From Proteopedia
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Revision as of 12:41, 30 October 2007
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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 ... [(full description)]
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]. Structure known Active Site: MN2. 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
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