› 2vem

X-ray diffraction
2.2Å resolution

Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties

Released:
DOI: 10.2210/pdb2vem/pdb
PDB entry 2vem coloured by chain, front view.
PDB entry 2vem coloured by chain, side view.
PDB entry 2vem coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Structure-based protein engineering efforts with a monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties.
Alahuhta M, Salin M, Casteleijn MG, Kemmer C, El-Sayed I, Augustyns K, Neubauer P, Wierenga RK
Protein Eng Des Sel 21 257-66 (2008)
PMID: 18239072

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase, glycosomal Chains: A, B
Molecule details ›
Chains: A, B
Length: 238 amino acids
Theoretical weight: 25.66 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04789 (Residues: 2-250; Coverage: 95%)
Sequence domains: Triosephosphate isomerase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand BBR 2 x BBR
Ligand TBU 1 x TBU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21
Unit cell:
a: 45.8Å b: 86.9Å c: 56.4Å
α: 90° β: 97.2° γ: 90°
R-values:
R R work R free
0.196 0.193 0.247
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.
Currin et al. (2015)
1 more