› 3l7r

X-ray diffraction
2.4Å resolution

crystal structure of MetE from streptococcus mutans

Released:
DOI: 10.2210/pdb3l7r/pdb
PDB entry 3l7r coloured by chain, front view.
PDB entry 3l7r coloured by chain, side view.
PDB entry 3l7r coloured by chain, top view.
Source organism: Streptococcus mutans UA159
Primary publication:
Crystal structures of cobalamin-independent methionine synthase (MetE) from Streptococcus mutans: a dynamic zinc-inversion model.
Fu TM, Almqvist J, Liang YH, Li L, Huang Y, Su XD
J Mol Biol 412 688-97 (2011)
PMID: 21840320

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-184020 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 779 amino acids
Theoretical weight: 87.8 KDa
Source organism: Streptococcus mutans UA159
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8CWX6 (Residues: 1-745; Coverage: 100%)
Gene names: SMU_873, metE
Sequence domains:
Structure domains: TIM Barrel

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P21
Unit cell:
a: 52.913Å b: 99.36Å c: 77.448Å
α: 90° β: 94.95° γ: 90°
R-values:
R R work R free
0.204 0.2 0.262
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Computational analysis of cysteine and methionine metabolism and its regulation in dairy starter and related bacteria.
Liu et al. (2012)
7 more

1 mention without citation

Redox regulation by reversible protein S-thiolation in Gram-positive bacteria.
Imber et al. (2019)