› 1jg1

X-ray diffraction
1.2Å resolution

Crystal Structure of L-isoaspartyl (D-aspartyl) O-methyltransferase with S-ADENOSYL-L-HOMOCYSTEINE

Released:
DOI: 10.2210/pdb1jg1/pdb
PDB entry 1jg1 coloured by chain, front view.
PDB entry 1jg1 coloured by chain, side view.
PDB entry 1jg1 coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
Crystal structure of a protein repair methyltransferase from Pyrococcus furiosus with its L-isoaspartyl peptide substrate.
Griffith SC, Sawaya MR, Boutz DR, Thapar N, Katz JE, Clarke S, Yeates TO
J Mol Biol 313 1103-16 (2001)
PMID: 11700066

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186343 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-L-isoaspartate O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 235 amino acids
Theoretical weight: 26.61 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TZR3 (Residues: 1-219; Coverage: 100%)
Gene names: PF1922, pcm
Sequence domains: Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT)
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P212121
Unit cell:
a: 39.16Å b: 52.522Å c: 96.636Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.142 0.2
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Aging as war between chemical and biochemical processes: protein methylation and the recognition of age-damaged proteins for repair.
Clarke S. (2003)
3 more

5 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
4 more