2iae
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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 with MN and ADD as ligands. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 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 Nov 12 22:42:45 2007