› 1q7q

X-ray diffraction
3.1Å resolution

Cobalamin-dependent methionine synthase (1-566) from T. maritima (Oxidized, Orthorhombic)

Released:
DOI: 10.2210/pdb1q7q/pdb
PDB entry 1q7q coloured by chain, front view.
PDB entry 1q7q coloured by chain, side view.
PDB entry 1q7q coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase.
Evans JC, Huddler DP, Hilgers MT, Romanchuk G, Matthews RG, Ludwig ML
Proc Natl Acad Sci U S A 101 3729-36 (2004)
PMID: 14752199

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194488 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 566 amino acids
Theoretical weight: 63.63 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9WYA5 (Residues: 1-566; Coverage: 74%)
Gene name: TM_0268
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: P212121
Unit cell:
a: 92.583Å b: 169.022Å c: 174.276Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.253 0.221 0.265
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Acetogenesis and the Wood-Ljungdahl pathway of CO(2) fixation.
Ragsdale et al. (2008)
12 more

1 mention without citation

Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase.
Evans et al. (2004)