› 1vbf

X-ray diffraction
2.8Å resolution

Crystal structure of protein L-isoaspartate O-methyltransferase homologue from Sulfolobus tokodaii

Released:
DOI: 10.2210/pdb1vbf/pdb
PDB entry 1vbf coloured by chain, front view.
PDB entry 1vbf coloured by chain, side view.
PDB entry 1vbf coloured by chain, top view.
Source organism: Sulfurisphaera tokodaii
Primary publication:
How oligomerization contributes to the thermostability of an archaeon protein. Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii.
Tanaka Y, Tsumoto K, Yasutake Y, Umetsu M, Yao M, Fukada H, Tanaka I, Kumagai I
J Biol Chem 279 32957-67 (2004)
PMID: 15169774

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:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188824 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
protein-L-isoaspartate(D-aspartate) O-methyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 231 amino acids
Theoretical weight: 26.38 KDa
Source organism: Sulfurisphaera tokodaii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q972K9 (Residues: 2-231; Coverage: 100%)
Gene names: ST1123, STK_11230, pcm
Sequence domains: Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT)
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: F23
Unit cell:
a: 277.803Å b: 277.803Å c: 277.803Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.255
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Posttranslational protein modification in Archaea.
Eichler et al. (2005)
3 more