2iae

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[[Image:2iae.jpg|left|200px]]<br /><applet load="2iae" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2iae.jpg|left|200px]]
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caption="2iae, resolution 3.50&Aring;" />
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'''Crystal structure of a protein phosphatase 2A (PP2A) holoenzyme.'''<br />
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{{Structure
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|PDB= 2iae |SIZE=350|CAPTION= <scene name='initialview01'>2iae</scene>, resolution 3.50&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=ADD:2,6,8-TRIMETHYL-3-AMINO-9-BENZYL-9-METHOXYNONANOIC ACID'>ADD</scene>
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|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]
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|GENE= Ppp2r1a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]), PPP2R5C, KIAA0044 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), PPP2CA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal structure of a protein phosphatase 2A (PP2A) holoenzyme.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2IAE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=ADD:'>ADD</scene> 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IAE OCA].
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2IAE is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IAE OCA].
==Reference==
==Reference==
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Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme., Cho US, Xu W, Nature. 2007 Jan 4;445(7123):53-7. Epub 2006 Nov 1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17086192 17086192]
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Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme., Cho US, Xu W, Nature. 2007 Jan 4;445(7123):53-7. Epub 2006 Nov 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17086192 17086192]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: tumor suppressor]]
[[Category: tumor suppressor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:50:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:27:09 2008''

Revision as of 15:27, 20 March 2008


PDB ID 2iae

Drag the structure with the mouse to rotate
, resolution 3.50Å
Ligands: and
Gene: Ppp2r1a (Mus musculus), PPP2R5C, KIAA0044 (Homo sapiens), PPP2CA (Homo sapiens)
Activity: Phosphoprotein phosphatase, with EC number 3.1.3.16
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a protein phosphatase 2A (PP2A) holoenzyme.


Overview

Protein phosphatase 2A (PP2A) is a principal Ser/Thr phosphatase, the deregulation of which is associated with multiple human cancers, Alzheimer's disease and increased susceptibility to pathogen infections. How PP2A is structurally organized and functionally regulated remains unclear. Here we report the crystal structure of an AB'C heterotrimeric PP2A holoenzyme. The structure reveals that the HEAT repeats of the scaffold A subunit form a horseshoe-shaped fold, holding the catalytic C and regulatory B' subunits together on the same side. The regulatory B' subunit forms pseudo-HEAT repeats and interacts with the C subunit near the active site, thereby defining substrate specificity. The methylated carboxy-terminal tail of the C subunit interacts with a highly negatively charged region at the interface between A and B' subunits, suggesting that the C-terminal carboxyl methylation of the C subunit promotes B' subunit recruitment by neutralizing charge repulsion. Together, our structural results establish a crucial foundation for understanding PP2A assembly, substrate recruitment and regulation.

About this Structure

2IAE is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme., Cho US, Xu W, Nature. 2007 Jan 4;445(7123):53-7. Epub 2006 Nov 1. PMID:17086192

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