1a6q
From Proteopedia
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|PDB= 1a6q |SIZE=350|CAPTION= <scene name='initialview01'>1a6q</scene>, resolution 2.0Å | |PDB= 1a6q |SIZE=350|CAPTION= <scene name='initialview01'>1a6q</scene>, resolution 2.0Å | ||
|SITE= <scene name='pdbsite=MN2:Mn+2++Binding+Sites'>MN2</scene> | |SITE= <scene name='pdbsite=MN2:Mn+2++Binding+Sites'>MN2</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> | + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a6q OCA], [http://www.ebi.ac.uk/pdbsum/1a6q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a6q RCSB]</span> | ||
}} | }} | ||
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[[Category: Das, A K.]] | [[Category: Das, A K.]] | ||
[[Category: Helps, N R.]] | [[Category: Helps, N R.]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: PO4]] | ||
[[Category: catalytic mechanism]] | [[Category: catalytic mechanism]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:34:28 2008'' |
Revision as of 15:34, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Phosphoprotein phosphatase, with EC number 3.1.3.16 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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