1rjf

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Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activityStructure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity

Structural highlights

1rjf is a 3 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LCMT1_YEAST Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues. Acts on the two major protein phosphatase 2A catalytic subunits, PPH21 and PPH22.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. Wu J, Tolstykh T, Lee J, Boyd K, Stock JB, Broach JR. Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic subunit promotes its functional association with regulatory subunits in vivo. EMBO J. 2000 Nov 1;19(21):5672-81. PMID:11060018 doi:http://dx.doi.org/10.1093/emboj/19.21.5672
  2. Kalhor HR, Luk K, Ramos A, Zobel-Thropp P, Clarke S. Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity responsible for modification of the major forms of protein phosphatase 2A in yeast. Arch Biochem Biophys. 2001 Nov 15;395(2):239-45. PMID:11697862 doi:http://dx.doi.org/10.1006/abbi.2001.2558

1rjf, resolution 2.25Å

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OCA