› 6bm5

X-ray diffraction
1.5Å resolution

Crystal Structure of the MetH Reactivation Domain bound to AdoMet

Released:
DOI: 10.2210/pdb6bm5/pdb
PDB entry 6bm5 coloured by chain, front view.
PDB entry 6bm5 coloured by chain, side view.
PDB entry 6bm5 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Water-Mediated Carbon-Oxygen Hydrogen Bonding Facilitates S-Adenosylmethionine Recognition in the Reactivation Domain of Cobalamin-Dependent Methionine Synthase.
Fick RJ, Clay MC, Vander Lee L, Scheiner S, Al-Hashimi H, Trievel RC
Biochemistry 57 3733-3740 (2018)
PMID: 29733595

Function and Biology Details

Reaction catalysed: 
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + 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-537098 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methionine synthase Chain: A
Molecule details ›
Chain: A
Length: 333 amino acids
Theoretical weight: 37.89 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P13009 (Residues: 897-1227; Coverage: 27%)
Gene names: JW3979, b4019, metH
Sequence domains: Vitamin B12 dependent methionine synthase, activation domain
Structure domains:

Ligands and Environments


Cofactor: Ligand SAM 1 x SAM
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 38.098Å b: 61.669Å c: 139.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.148 0.146 0.194
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Structural basis for stereoselective dehydration and hydrogen-bonding catalysis by the SAM-dependent pericyclase LepI.
Cai et al. (2019)
1 more

1 mention without citation

Structure of full-length cobalamin-dependent methionine synthase and cofactor loading captured in crystallo.
Mendoza et al. (2023)