› 1xpg

X-ray diffraction
2.59Å resolution

Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Methyltetrahydrofolate

Released:
DOI: 10.2210/pdb1xpg/pdb
PDB entry 1xpg coloured by chain, front view.
PDB entry 1xpg coloured by chain, side view.
PDB entry 1xpg coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication.
Pejchal R, Ludwig ML
PLoS Biol 3 e31 (2005)
PMID: 15630480

Function and Biology Details

Reaction catalysed: 
5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194762 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 765 amino acids
Theoretical weight: 89.99 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X112 (Residues: 2-732; Coverage: 100%)
Gene names: TM_1286, metE
Sequence domains:
Structure domains: TIM Barrel

Ligands and Environments

4 bound ligands:
Ligand SO4 3 x SO4
Ligand ZN 2 x ZN
Ligand C2F 2 x C2F
Ligand MRY 2 x MRY
1 modified residue:
Ligand MSE 34 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P21212
Unit cell:
a: 163.948Å b: 159.303Å c: 64.449Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.248
Expression system: Escherichia coli

Quick links

Citations

8 review citations

The structural and functional diversity of metabolite-binding riboswitches.
Roth et al. (2009)
7 more

2 mentions without citation

Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication.
Pejchal et al. (2005)
1 more