› 2vfe

X-ray diffraction
2.2Å resolution

Crystal structure of F96S mutant of Plasmodium falciparum triosephosphate isomerase with 3- phosphoglycerate bound at the dimer interface

Released:
DOI: 10.2210/pdb2vfe/pdb
PDB entry 2vfe coloured by chain, front view.
PDB entry 2vfe coloured by chain, side view.
PDB entry 2vfe 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

2 bound ligands:
Ligand 3PG 2 x 3PG
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 53.843Å b: 50.872Å c: 87.067Å
α: 90° β: 92.5° γ: 90°
R-values:
R R work R free
0.221 0.218 0.276
Expression system: Escherichia coli

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Citations

3 review citations

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