› 3uj7

X-ray diffraction
1.55Å resolution

Phosphoethanolamine methyltransferase from Plasmodium falciparum in complex with SAM and PO4

Released:
DOI: 10.2210/pdb3uj7/pdb
PDB entry 3uj7 coloured by chain, front view.
PDB entry 3uj7 coloured by chain, side view.
PDB entry 3uj7 coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Structure and reaction mechanism of phosphoethanolamine methyltransferase from the malaria parasite Plasmodium falciparum: an antiparasitic drug target.
Lee SG, Kim Y, Alpert TD, Nagata A, Jez JM
J Biol Chem 287 1426-34 (2012)
PMID: 22117061

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + ethanolamine phosphate = S-adenosyl-L-homocysteine + N-methylethanolamine phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180355 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoethanolamine N-methyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 266 amino acids
Theoretical weight: 31.08 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8IDQ9 (Residues: 1-266; Coverage: 100%)
Gene names: PF3D7_1343000, PMT
Sequence domains: Methyltransferase domain
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAM 2 x SAM
1 bound ligand:
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P2
Unit cell:
a: 77.035Å b: 44.13Å c: 88.411Å
α: 90° β: 108.48° γ: 90°
R-values:
R R work R free
0.167 0.166 0.185
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Architectures, mechanisms and molecular evolution of natural product methyltransferases.
Liscombe et al. (2012)
6 more

4 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
3 more