› 1rjd

X-ray diffraction
1.8Å resolution

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

Released:
DOI: 10.2210/pdb1rjd/pdb
PDB entry 1rjd coloured by chain, front view.
PDB entry 1rjd coloured by chain, side view.
PDB entry 1rjd coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of protein phosphatase methyltransferase 1 (PPM1), a leucine carboxyl methyltransferase involved in the regulation of protein phosphatase 2A activity.
Leulliot N, Quevillon-Cheruel S, Sorel I, Li de La Sierra-Gallay I, Collinet B, Graille M, Blondeau K, Bettache N, Poupon A, Janin J, van Tilbeurgh H
J Biol Chem 279 8351-8 (2004)
PMID: 14660564

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine = S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169993 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine carboxyl methyltransferase 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 334 amino acids
Theoretical weight: 38.57 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04081 (Residues: 1-328; Coverage: 100%)
Gene names: PPM1, YDR435C
Sequence domains: Leucine carboxyl methyltransferase
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAM 3 x SAM
2 bound ligands:
Ligand BME 6 x BME
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P65
Unit cell:
a: 110.683Å b: 110.683Å c: 165.879Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.178 0.215
Expression system: Escherichia coli

Quick links

Citations

24 review citations

PP2A holoenzyme assembly: in cauda venenum (the sting is in the tail).
Janssens et al. (2008)
23 more

3 mentions without citation

Structural basis of tRNA modification with CO2 fixation and methylation by wybutosine synthesizing enzyme TYW4.
Suzuki et al. (2009)
2 more