2iae: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 2iae |SIZE=350|CAPTION= <scene name='initialview01'>2iae</scene>, resolution 3.50Å | |PDB= 2iae |SIZE=350|CAPTION= <scene name='initialview01'>2iae</scene>, resolution 3.50Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ACB:3-METHYL-ASPARTIC+ACID'>ACB</scene>, <scene name='pdbligand=ADD:2,6,8-TRIMETHYL-3-AMINO-9-BENZYL-9-METHOXYNONANOIC+ACID'>ADD</scene>, <scene name='pdbligand=CAB:4-CARBOXY-4-AMINOBUTANAL'>CAB</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MAA:N-METHYLALANINE'>MAA</scene>, <scene name='pdbligand=MLL:METHYL+L-LEUCINATE'>MLL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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= 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]) | |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]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1b3u|1B3U]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iae OCA], [http://www.ebi.ac.uk/pdbsum/2iae PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2iae RCSB]</span> | |||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Cho, U S.]] | [[Category: Cho, U S.]] | ||
[[Category: Xu, W.]] | [[Category: Xu, W.]] | ||
[[Category: b56]] | [[Category: b56]] | ||
[[Category: crystal structure]] | [[Category: crystal structure]] | ||
| Line 36: | Line 37: | ||
[[Category: tumor suppressor]] | [[Category: tumor suppressor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:41:37 2008'' | ||
Revision as of 03:41, 31 March 2008
| |||||||
| , resolution 3.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , , | ||||||
| Gene: | Ppp2r1a (Mus musculus), PPP2R5C, KIAA0044 (Homo sapiens), PPP2CA (Homo sapiens) | ||||||
| Activity: | Phosphoprotein phosphatase, with EC number 3.1.3.16 | ||||||
| Related: | 1B3U
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a protein phosphatase 2A (PP2A) holoenzyme.
OverviewOverview
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 StructureAbout this Structure
2IAE is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Mon Mar 31 03:41:37 2008