› 3bq5

X-ray diffraction
2Å resolution

Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Homocysteine (Monoclinic)

Released:
DOI: 10.2210/pdb3bq5/pdb
PDB entry 3bq5 coloured by chain, front view.
PDB entry 3bq5 coloured by chain, side view.
PDB entry 3bq5 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Metal active site elasticity linked to activation of homocysteine in methionine synthases.
Koutmos M, Pejchal R, Bomer TM, Matthews RG, Smith JL, Ludwig ML
Proc Natl Acad Sci U S A 105 3286-91 (2008)
PMID: 18296644

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: 766 amino acids
Theoretical weight: 89.41 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X112 (Residues: 2-734; Coverage: 100%)
Gene names: TM_1286, metE
Sequence domains:
Structure domains: TIM Barrel

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand HCS 2 x HCS
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 73.229Å b: 107.164Å c: 107.667Å
α: 90° β: 108.96° γ: 90°
R-values:
R R work R free
0.218 0.217 0.24
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Cobalamin-dependent and cobamide-dependent methyltransferases.
Matthews et al. (2008)
4 more

2 mentions without citation

Metal active site elasticity linked to activation of homocysteine in methionine synthases.
Koutmos et al. (2008)
1 more