› 2v2h

X-ray diffraction
1.18Å resolution

The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM

Released:
DOI: 10.2210/pdb2v2h/pdb
PDB entry 2v2h coloured by chain, front view.
PDB entry 2v2h coloured by chain, side view.
PDB entry 2v2h coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Structural studies show that the A178L mutation in the C-terminal hinge of the catalytic loop-6 of triosephosphate isomerase (TIM) induces a closed-like conformation in dimeric and monomeric TIM.
Alahuhta M, Casteleijn MG, Neubauer P, Wierenga RK
Acta Crystallogr D Biol Crystallogr 64 178-88 (2008)
PMID: 18219118

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 trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138177 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 242 amino acids
Theoretical weight: 26.08 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04789 (Residues: 1-250; Coverage: 97%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand PGA 3 x PGA
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: C2
Unit cell:
a: 68.26Å b: 117.99Å c: 81.77Å
α: 90° β: 95.84° γ: 90°
R-values:
R R work R free
0.139 not available 0.187
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

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)
9 other articles