title: The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A.
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.
authors.affiliation: Institute of Structural and Molecular Biology, University College London, England.
authors.forename: Meng Lin
authors.initials: ML
authors.lastname: Tsai
authors.forename: Nora
authors.initials: N
authors.lastname: Cronin
authors.forename: Snezana
authors.initials: S
authors.lastname: Djordjevic
mesh_terms: D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011497:Protein O-Methyltransferase / Q000737:chemistry / Q000378:metabolism; D054648:Protein Phosphatase 2 / Q000737:chemistry* / Q000378:metabolism; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D016415:Sequence Alignment; D040681:Structural Homology, Protein
chemical_list: C524761:LCMT1 protein, human; D011497:Protein O-Methyltransferase; D054648:Protein Phosphatase 2