2ie3
From Proteopedia
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|PDB= 2ie3 |SIZE=350|CAPTION= <scene name='initialview01'>2ie3</scene>, resolution 2.8Å | |PDB= 2ie3 |SIZE=350|CAPTION= <scene name='initialview01'>2ie3</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | + | |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=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=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=9606 Homo sapiens]), PPP2CA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2ie4|2IE4]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ie3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ie3 OCA], [http://www.ebi.ac.uk/pdbsum/2ie3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ie3 RCSB]</span> | ||
}} | }} | ||
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[[Category: Xing, Y.]] | [[Category: Xing, Y.]] | ||
[[Category: Xu, Y.]] | [[Category: Xu, Y.]] | ||
| - | [[Category: MN]] | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
| - | ''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 03:43:05 2008'' |
Revision as of 00:43, 31 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , , , | ||||||
| Gene: | PPP2R1A (Homo sapiens), PPP2CA (Homo sapiens) | ||||||
| Activity: | Phosphoprotein phosphatase, with EC number 3.1.3.16 | ||||||
| Related: | 2IE4
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor-inducing Toxins
Overview
The serine/threonine phosphatase protein phosphatase 2A (PP2A) plays an essential role in many aspects of cellular functions and has been shown to be an important tumor suppressor. The core enzyme of PP2A comprises a 65 kDa scaffolding subunit and a 36 kDa catalytic subunit. Here we report the crystal structures of the PP2A core enzyme bound to two of its inhibitors, the tumor-inducing agents okadaic acid and microcystin-LR, at 2.6 and 2.8 A resolution, respectively. The catalytic subunit recognizes one end of the elongated scaffolding subunit by interacting with the conserved ridges of HEAT repeats 11-15. Formation of the core enzyme forces the scaffolding subunit to undergo pronounced structural rearrangement. The scaffolding subunit exhibits considerable conformational flexibility, which is proposed to play an essential role in PP2A function. These structures, together with biochemical analyses, reveal significant insights into PP2A function and serve as a framework for deciphering the diverse roles of PP2A in cellular physiology.
About this Structure
2IE3 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins., Xing Y, Xu Y, Chen Y, Jeffrey PD, Chao Y, Lin Z, Li Z, Strack S, Stock JB, Shi Y, Cell. 2006 Oct 20;127(2):341-53. PMID:17055435
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