› 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 5him coloured by chain and viewed from the front.
PDB 5him coloured by chain and viewed from the side.
PDB 5him coloured by chain and viewed from the top.
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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (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

2 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)
1 more