› 1k98

X-ray diffraction
3.75Å resolution

AdoMet complex of MetH C-terminal fragment

Released:
DOI: 10.2210/pdb1k98/pdb
PDB entry 1k98 coloured by chain, front view.
PDB entry 1k98 coloured by chain, side view.
PDB entry 1k98 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Domain alternation switches B(12)-dependent methionine synthase to the activation conformation.
Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG, Ludwig ML
Nat Struct Biol 9 53-6 (2002)
PMID: 11731805

Function and Biology Details

Reaction catalysed: 
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146429 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine synthase Chain: A
Molecule details ›
Chain: A
Length: 577 amino acids
Theoretical weight: 64.86 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P13009 (Residues: 651-1227; Coverage: 47%)
Gene names: JW3979, b4019, metH
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand B12 1 x B12
1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P43212
Unit cell:
a: 108.503Å b: 108.503Å c: 146.474Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.311 0.308 0.363
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase.
Gulick AM. (2009)
9 more

6 mentions without citation

Age-dependent decrease and alternative splicing of methionine synthase mRNA in human cerebral cortex and an accelerated decrease in autism.
Muratore et al. (2013)
5 more