› 2vfd

X-ray diffraction
1.4Å resolution

Crystal structure of the F96S mutant of Plasmodium falciparum triosephosphate isomerase

Released:
DOI: 10.2210/pdb2vfd/pdb
PDB entry 2vfd coloured by chain, front view.
PDB entry 2vfd coloured by chain, side view.
PDB entry 2vfd coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Biochemical and structural characterization of residue 96 mutants of Plasmodium falciparum triosephosphate isomerase: active-site loop conformation, hydration and identification of a dimer-interface ligand-binding site.
Gayathri P, Banerjee M, Vijayalakshmi A, Balaram H, Balaram P, Murthy MR
Acta Crystallogr D Biol Crystallogr 65 847-57 (2009)
PMID: 19622869

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170466 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 248 amino acids
Theoretical weight: 27.94 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q07412 (Residues: 1-248; Coverage: 100%)
Gene name: TPI
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 53.423Å b: 50.698Å c: 89.188Å
α: 90° β: 92.17° γ: 90°
R-values:
R R work R free
0.166 0.165 0.188
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Triosephosphate isomerase: a highly evolved biocatalyst.
Wierenga et al. (2010)
2 more

1 mention without citation

Structure of triosephosphate isomerase from Cryptosporidium parvum.
Nguyen et al. (2011)