› 1tsi

X-ray diffraction
2.84Å resolution

STRUCTURE OF THE COMPLEX BETWEEN TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE AND N-HYDROXY-4-PHOSPHONO-BUTANAMIDE: BINDING AT THE ACTIVE SITE DESPITE AN "OPEN" FLEXIBLE LOOP

Released:
DOI: 10.2210/pdb1tsi/pdb
PDB entry 1tsi coloured by chain, front view.
PDB entry 1tsi coloured by chain, side view.
PDB entry 1tsi coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Structure of the complex between trypanosomal triosephosphate isomerase and N-hydroxy-4-phosphono-butanamide: binding at the active site despite an "open" flexible loop conformation.
Verlinde CL, Witmans CJ, Pijning T, Kalk KH, Hol WG, Callens M, Opperdoes FR
Protein Sci 1 1578-84 (1992)
PMID: 1304889

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-138176 (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: 26.95 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Not provided
UniProt:
  • Canonical: P04789 (Residues: 1-250; Coverage: 100%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand 4PB 1 x 4PB
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 113.34Å b: 97.15Å c: 46.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.115 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

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

4 mentions without citation

The critical role of the loops of triosephosphate isomerase for its oligomerization, dynamics, and functionality.
Katebi et al. (2014)
3 more