› 3lbf

X-ray diffraction
1.8Å resolution

Crystal structure of Protein L-isoaspartyl methyltransferase from Escherichia coli

Released:
DOI: 10.2210/pdb3lbf/pdb
PDB entry 3lbf coloured by chain, front view.
PDB entry 3lbf coloured by chain, side view.
PDB entry 3lbf coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystal structure of the protein L-isoaspartyl methyltransferase from Escherichia coli.
Fang P, Li X, Wang J, Xing L, Gao Y, Niu L, Teng M
Cell Biochem Biophys 58 163-7 (2010)
PMID: 20857228

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-L-isoaspartate O-methyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 210 amino acids
Theoretical weight: 23.49 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7A5 (Residues: 1-208; Coverage: 100%)
Gene names: JW2713, b2743, pcm
Sequence domains: Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT)
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 4 x SAH
2 bound ligands:
Ligand PO4 6 x PO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P1
Unit cell:
a: 52.3Å b: 55.06Å c: 67.49Å
α: 74° β: 74.7° γ: 85.57°
R-values:
R R work R free
0.215 0.213 0.247
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Crystal structure and activity of protein L-isoaspartyl-O-methyltransferase from Vibrio cholerae, and the effect of AdoHcy binding.
Chatterjee et al. (2015)
2 more

2 mentions without citation

Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
Houben et al. (2020)
1 more