Xing YN, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi YG. Structural Mechnism of Demethylation and Inactivation of Protein Phosphatase 2A. CELL 133: 154-163, 2008

root 提交于 周日, 10/31/2021 - 01:47
Abstract Protein phosphatase 2A (PP2A) is an important serine/threonine phosphatase that plays a role in many biological processes. Reversible carboxyl methylation of the PP2A catalytic subunit is an essential regulatory mechanism for its function. Demethylation and negative regulation of PP2A is mediated by a PP2A-specific methylesterase PME-1, which is conserved from yeast to humans. However, the underlying mechanism of PME-1 function remains enigmatic. Here we report the crystal structures of PME-1 by itself and in complex with a PP2A heterodimeric core enzyme. The structures reveal that PME-1 directly binds to the active site of PP2A and that this interaction results in the activation of PME-1 by rearranging the catalytic triad into an active conformation. Strikingly, these interactio......

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