› 3kof

X-ray diffraction
1.9Å resolution

Crystal structure of the double mutant F178Y/R181E of E.coli transaldolase B

Released:
DOI: 10.2210/pdb3kof/pdb
PDB entry 3kof coloured by chain, front view.
PDB entry 3kof coloured by chain, side view.
PDB entry 3kof coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Redesigning the active site of transaldolase TalB from Escherichia coli: new variants with improved affinity towards nonphosphorylated substrates.
Schneider S, Gutiérrez M, Sandalova T, Schneider G, Clapés P, Sprenger GA, Samland AK
Chembiochem 11 681-90 (2010)
PMID: 20148428

Function and Biology Details

Reaction catalysed: 
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141669 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase B Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 37.45 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A870 (Residues: 1-317; Coverage: 100%)
Gene names: JW0007, b0008, talB, yaaK
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 66.404Å b: 86.397Å c: 130.745Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.203 0.248
Expression system: Escherichia coli

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Citations

11 review citations

Advanced biotechnology: metabolically engineered cells for the bio-based production of chemicals and fuels, materials, and health-care products.
Becker et al. (2015)
10 more