› 5him

X-ray diffraction
2.34Å resolution

Crystal structure of glycine sarcosine N-methyltransferase from Methanohalophilus portucalensis in complex with S-adenosylhomocysteine and dimethylglycine

Released:
DOI: 10.2210/pdb5him/pdb
PDB entry 5him coloured by chain, front view.
PDB entry 5him coloured by chain, side view.
PDB entry 5him coloured by chain, top view.
Source organism: Methanohalophilus portucalensis FDF-1
Primary publication:
Structural Analysis of Glycine Sarcosine N-methyltransferase from Methanohalophilus portucalensis Reveals Mechanistic Insights into the Regulation of Methyltransferase Activity.
Lee YR, Lin TS, Lai SJ, Liu MS, Lai MC, Chan NL
Sci Rep 6 38071 (2016)
PMID: 27934872

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + sarcosine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123622 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methyltransferase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 284 amino acids
Theoretical weight: 32.8 KDa
Source organism: Methanohalophilus portucalensis FDF-1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: F6KV61 (Residues: 1-263; Coverage: 100%)
Gene names: EFE41_00900, MPF_0823, SAMN06264941_0527, gsmt
Sequence domains: Methyltransferase domain
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
2 bound ligands:
Ligand DMG 1 x DMG
Ligand EDO 6 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: I222
Unit cell:
a: 51.975Å b: 121.219Å c: 131.686Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.156 0.207
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

A simplified characterization of S-adenosyl-l-methionine-consuming enzymes with 1-Step EZ-MTase: a universal and straightforward coupled-assay for in vitro and in vivo setting.
Burgos et al. (2017)
2 more