› 2oma

X-ray diffraction
2.15Å resolution

Crystallographic analysis of a chemically modified triosephosphate isomerase from Trypanosoma cruzi with dithiobenzylamine (DTBA)

Released:
DOI: 10.2210/pdb2oma/pdb
PDB entry 2oma coloured by chain, front view.
PDB entry 2oma coloured by chain, side view.
PDB entry 2oma coloured by chain, top view.
Source organism: Trypanosoma cruzi
Primary publication:
Perturbation of the dimer interface of triosephosphate isomerase and its effect on Trypanosoma cruzi.
Olivares-Illana V, Rodríguez-Romero A, Becker I, Berzunza M, García J, Pérez-Montfort R, Cabrera N, López-Calahorra F, de Gómez-Puyou MT, Gómez-Puyou A
PLoS Negl Trop Dis 1 e1 (2007)
PMID: 17989778

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-156485 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 27.35 KDa
Source organism: Trypanosoma cruzi
Expression system: Escherichia coli
UniProt:
  • Canonical: P52270 (Residues: 2-251; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand SO4 9 x SO4
Ligand PEG 3 x PEG
Ligand PGE 1 x PGE
1 modified residue:
Ligand CS1 2 x CS1

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 43.206Å b: 75.337Å c: 146.427Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.25
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

3 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
2 more