› 2vfg

X-ray diffraction
1.95Å resolution

Crystal structure of the F96H mutant of Plasmodium falciparum triosephosphate isomerase with 3-phosphoglycerate bound at the dimer interface

Released:
DOI: 10.2210/pdb2vfg/pdb
PDB entry 2vfg coloured by chain, front view.
PDB entry 2vfg coloured by chain, side view.
PDB entry 2vfg 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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 248 amino acids
Theoretical weight: 27.99 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 3PG 4 x 3PG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 90.197Å b: 47.136Å c: 109.167Å
α: 90° β: 96.65° γ: 90°
R-values:
R R work R free
0.21 0.208 0.248
Expression system: Escherichia coli

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Citations

3 review citations

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