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1a6q

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==Overview==
==Overview==
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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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9003755 (full description)]]
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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==
==About this Structure==
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1A6Q is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with MN and PO4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16]]. Structure known Active Site: MN2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A6Q OCA]].
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1A6Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MN and PO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] Structure known Active Site: MN2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A6Q OCA].
==Reference==
==Reference==
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[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:45:49 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:48:09 2007''

Revision as of 10:42, 5 November 2007


1a6q, resolution 2.0Å

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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 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 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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