› 1lyx

X-ray diffraction
1.9Å resolution

Plasmodium Falciparum Triosephosphate Isomerase (PfTIM)-Phosphoglycolate complex

Released:
DOI: 10.2210/pdb1lyx/pdb
PDB entry 1lyx coloured by chain, front view.
PDB entry 1lyx coloured by chain, side view.
PDB entry 1lyx coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Structure of the Plasmodium falciparum triosephosphate isomerase-phosphoglycolate complex in two crystal forms: characterization of catalytic loop open and closed conformations in the ligand-bound state.
Parthasarathy S, Ravindra G, Balaram H, Balaram P, Murthy MR
Biochemistry 41 13178-88 (2002)
PMID: 12403619

Function and Biology Details

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

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 Chain: A
Molecule details ›
Chain: A
Length: 248 amino acids
Theoretical weight: 28 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 PGA 1 x PGA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 88.242Å b: 63.437Å c: 53.886Å
α: 90° β: 117.74° γ: 90°
R-values:
R R work R free
0.18 0.18 0.21
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

9 mentions without citation

Heterologous expression of plasmodial proteins for structural studies and functional annotation.
Birkholtz et al. (2008)
8 more