› 5dmn

X-ray diffraction
2.89Å resolution

Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Apo form

Released:
DOI: 10.2210/pdb5dmn/pdb
PDB entry 5dmn coloured by chain, front view.
PDB entry 5dmn coloured by chain, side view.
PDB entry 5dmn coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystal structure of the homocysteine methyltransferase MmuM from Escherichia coli.
Li K, Li G, Bradbury LM, Hanson AD, Bruner SD
Biochem J 473 277-84 (2016)
PMID: 26564203

Function and Biology Details

Reaction catalysed: 
S-methyl-L-methionine + L-homocysteine = 2 L-methionine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Homocysteine S-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 310 amino acids
Theoretical weight: 33.46 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: Q47690 (Residues: 1-310; Coverage: 100%)
Gene names: JW0253, b0261, mmuM, yagD
Sequence domains: Homocysteine S-methyltransferase
Structure domains: Homocysteine-binding-like domain

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21212
Unit cell:
a: 85.822Å b: 85.945Å c: 79.016Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.226 0.27
Expression system: Escherichia coli

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Citations

5 citation in other articles

Revisiting the methionine salvage pathway and its paralogues.
Sekowska et al. (2019)
4 more