› 4s2b

X-ray diffraction
1.46Å resolution

Covalent complex of E. coli transaldolase TalB with tagatose-6-phosphate

Released:
DOI: 10.2210/pdb4s2b/pdb
PDB entry 4s2b coloured by chain, front view.
PDB entry 4s2b coloured by chain, side view.
PDB entry 4s2b coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Novel mode of inhibition by D-tagatose 6-phosphate through a Heyns rearrangement in the active site of transaldolase B variants.
Stellmacher L, Sandalova T, Schneider S, Schneider G, Sprenger GA, Samland AK
Acta Crystallogr D Struct Biol 72 467-76 (2016)
PMID: 27050126

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141670 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase B Chains: A, B
Molecule details ›
Chains: A, B
Length: 337 amino acids
Theoretical weight: 37.48 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

2 bound ligands:
Ligand 44S 2 x 44S
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Spacegroup: P212121
Unit cell:
a: 67.308Å b: 91.699Å c: 130.987Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.152 0.185
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

The Differential Growth Inhibition of Phytophthora spp. Caused by the Rare Sugar Tagatose Is Associated With Species-Specific Metabolic and Transcriptional Changes.
Chahed et al. (2021)