2iae | pdb_00002iae

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

spinqualitylabelsall models 2iae, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2iae is a 8 chain structure with sequence from Homo sapiens, Microcystis aeruginosa and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5Å Ligands: 1ZN, ACB, DAL, DAM, FGA, MLL, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 2AAA_MOUSE The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Required for proper chromosome segregation and for centromeric localization of SGOL1 in mitosis (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Protein phosphatase 3D structures

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