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 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.
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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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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Barford, D.]]
[[Category: Barford, D.]]
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[[Category: Cohen, P.T.W.]]
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[[Category: Cohen, P T.W.]]
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[[Category: Das, A.K.]]
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[[Category: Das, A K.]]
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[[Category: Helps, N.R.]]
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[[Category: Helps, N R.]]
[[Category: MN]]
[[Category: MN]]
[[Category: PO4]]
[[Category: PO4]]
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[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:29:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:27 2008''

Revision as of 09:41, 21 February 2008


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 and 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

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