› 2y70

X-ray diffraction
2.3Å resolution

CRYSTALLOGRAPHIC STRUCTURE OF GM23, MUTANT G89D, AN EXAMPLE OF CATALYTIC MIGRATION FROM TIM TO THIAMIN PHOSPHATE SYNTHASE.

Released:
DOI: 10.2210/pdb2y70/pdb
PDB entry 2y70 coloured by chain, front view.
PDB entry 2y70 coloured by chain, side view.
PDB entry 2y70 coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Evolutionary walk between (β/α)(8) barrels: catalytic migration from triosephosphate isomerase to thiamin phosphate synthase.
Saab-Rincón G, Olvera L, Olvera M, Rudiño-Piñera E, Benites E, Soberón X, Morett E
J Mol Biol 416 255-70 (2012)
PMID: 22226942

Function and Biology Details

Reaction catalysed: 
D-glyceraldehyde 3-phosphate = glycerone phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 245 amino acids
Theoretical weight: 26.38 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: P04789 (Residues: 1-47, 49-250; Coverage: 97%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand ACT 17 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P32
Unit cell:
a: 109.444Å b: 109.444Å c: 95.24Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.199 0.23
Expression system: Escherichia coli

Quick links

Citations

3 review citations

A guide to the effects of a large portion of the residues of triosephosphate isomerase on catalysis, stability, druggability, and human disease.
Olivares-Illana et al. (2017)
2 more