› 4o6z

X-ray diffraction
2.98Å resolution

Crystal structure of serine hydroxymethyltransferase with covalently bound PLP Schiff-base from Plasmodium falciparum

Released:
DOI: 10.2210/pdb4o6z/pdb
PDB entry 4o6z coloured by chain, front view.
PDB entry 4o6z coloured by chain, side view.
PDB entry 4o6z coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
The structure of Plasmodium falciparum serine hydroxymethyltransferase reveals a novel redox switch that regulates its activities.
Chitnumsub P, Ittarat W, Jaruwat A, Noytanom K, Amornwatcharapong W, Pornthanakasem W, Chaiyen P, Yuthavong Y, Leartsakulpanich U
Acta Crystallogr D Biol Crystallogr 70 1517-27 (2014)
PMID: 24914963

Function and Biology Details

Reaction catalysed: 
5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184684 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine hydroxymethyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 480 amino acids
Theoretical weight: 54.12 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8I566 (Residues: 1-442; Coverage: 100%)
Gene names: PF3D7_1235600, SHMT
Sequence domains: Serine hydroxymethyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 3 x PLP
1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P61
Unit cell:
a: 254.947Å b: 254.947Å c: 61.399Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.224 0.27
Expression system: Escherichia coli

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Citations

1 review citation

Artemisinin-based antimalarial research: application of biotechnology to the production of artemisinin, its mode of action, and the mechanism of resistance of Plasmodium parasites.
Muangphrom et al. (2016)
6 other articles

5 mentions without citation

Dihydrofolate reductase, thymidylate synthase, and serine hydroxy methyltransferase: successful targets against some infectious diseases.
Shamshad et al. (2022)
4 more