X-ray diffraction
1.95Å resolution

Crystal structure of trans-aconitate methyltransferase from Agrobacterium tumefaciens

Entry authors: Chang C, Xu X, Zheng H, Savchenko A, Edwards AM, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + (E)-3-(methoxycarbonyl)pent-2-enedioate
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Trans-aconitate 2-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 259 amino acids
Theoretical weight: 29.12 KDa
Source organism: Agrobacterium fabrum str. C58
Expression system: Escherichia coli
  • Canonical: Q8UH15 (Residues: 1-256; Coverage: 100%)
Gene names: AGR_C_1589, Atu0870, tam
Sequence domains: Methyltransferase domain
Structure domains:

Ligands and Environments

Cofactor: Ligand SAH 2 x SAH
No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P65
Unit cell:
a: 103.097Å b: 103.097Å c: 107.457Å
α: 90° β: 90° γ: 120°
R R work R free
0.187 0.186 0.214
Expression system: Escherichia coli