› 2eg5

X-ray diffraction
2.2Å resolution

The structure of xanthosine methyltransferase

Released:
DOI: 10.2210/pdb2eg5/pdb
PDB entry 2eg5 coloured by chain, front view.
PDB entry 2eg5 coloured by chain, side view.
PDB entry 2eg5 coloured by chain, top view.
Source organism: Coffea canephora
Primary publication:
The structure of two N-methyltransferases from the caffeine biosynthetic pathway.
McCarthy AA, McCarthy JG
Plant Physiol 144 879-89 (2007)
PMID: 17434991

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + xanthosine = S-adenosyl-L-homocysteine + 7-methylxanthosine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107291 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
7-methylxanthosine synthase 1 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 372 amino acids
Theoretical weight: 41.89 KDa
Source organism: Coffea canephora
Expression system: Escherichia coli
UniProt:
  • Canonical: A4GE69 (Residues: 1-372; Coverage: 100%)
Gene names: GSCOC_T00036338001, XMT1
Sequence domains: SAM dependent carboxyl methyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 4 x SAH
1 bound ligand:
Ligand XTS 4 x XTS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 57.59Å b: 119.8Å c: 116.4Å
α: 90° β: 102.16° γ: 90°
R-values:
R R work R free
0.233 0.23 0.284
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Alkaloid biosynthesis: metabolism and trafficking.
Ziegler et al. (2008)
9 more

2 mentions without citation

Functional Diversification and Structural Origins of Plant Natural Product Methyltransferases.
Lashley et al. (2022)
1 more