› 4r6x

X-ray diffraction
2.55Å resolution

Plasmodium falciparum phosphoethanolamine methyltransferase D128A mutant in complex with S-adenosylhomocysteine and phosphoethanolamine

Released:
DOI: 10.2210/pdb4r6x/pdb
PDB 4r6x coloured by chain and viewed from the front.
PDB 4r6x coloured by chain and viewed from the side.
PDB 4r6x coloured by chain and viewed from the top.
Source organism: Plasmodium falciparum
Primary publication:
An Alternate Mechanism for the Methylation of Phosphoethanolamine Catalyzed by Plasmodium falciparum Phosphoethanolamine Methyltransferase.
Saen-Oon S, Lee SG, Jez JM, Guallar V
J. Biol. Chem. (2014)
PMID: 25288796

Function and Biology Details

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 type 11 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 258 amino acids
Theoretical weight: 30.11 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6T755 (Residues: 9-266; Coverage: 97%)
Gene name: PMT
Sequence domains: Methyltransferase domain
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments

2 bound ligands:
Ligand OPE 2 x OPE
Ligand SAH 2 x SAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P2
Unit cell:
a: 76.826Å b: 43.652Å c: 88.053Å
α: 90° β: 107.79° γ: 90°
R-values:
R R work R free
0.205 0.203 0.258
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 citation in other articles

High-resolution metabolomics to discover potential parasite-specific biomarkers in a Plasmodium falciparum erythrocytic stage culture system.
Park et al. (2015)
6 more

1 mention without citation

An alternative mechanism for the methylation of phosphoethanolamine catalyzed by Plasmodium falciparum phosphoethanolamine methyltransferase.
Saen-Oon et al. (2014)