151. The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A.
- Author
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Tsai ML, Cronin N, and Djordjevic S
- Subjects
- Amino Acid Sequence, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein O-Methyltransferase chemistry, Protein O-Methyltransferase metabolism, Protein Phosphatase 2 metabolism, Protein Structure, Quaternary, Protein Structure, Tertiary, Saccharomyces cerevisiae enzymology, Sequence Alignment, Structural Homology, Protein, Protein Phosphatase 2 chemistry
- Abstract
Leucine carboxyl methyltransferase 1 (LCMT1) methylates the terminal carboxyl group of the leucine 309 residue of human protein phosphatase 2A (PP2A). PP2A, a key regulator of many cellular processes, has recently generated additional interest as a potential cancer-therapeutic target. The status of PP2A methylation impacts upon the selection of the regulatory subunit by the PP2A core enzyme, thus directing its activity and subcellular localization. An X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet) has been solved to a resolution of 2 Å. The structure enables the postulation of a mode of interaction with protein phosphatase PP2A and provides a platform for further functional studies of the regulation of methylation of PP2A.
- Published
- 2011
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