Structural highlights
Function
[LCMT1_HUMAN] Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.[1]
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
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 A. 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.
The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A.,Tsai ML, Cronin N, Djordjevic S Acta Crystallogr D Biol Crystallogr. 2011 Jan;67(Pt 1):14-24. Epub 2010, Dec 16. PMID:21206058[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J. Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue. Biochemistry. 1999 Dec 14;38(50):16539-47. PMID:10600115
- ↑ Tsai ML, Cronin N, Djordjevic S. The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A. Acta Crystallogr D Biol Crystallogr. 2011 Jan;67(Pt 1):14-24. Epub 2010, Dec 16. PMID:21206058 doi:10.1107/S0907444910042204
