› 4e0c

X-ray diffraction
1.8Å resolution

1.8 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis (phosphate-free)

Released:
DOI: 10.2210/pdb4e0c/pdb
PDB entry 4e0c coloured by chain, front view.
PDB entry 4e0c coloured by chain, side view.
PDB entry 4e0c coloured by chain, top view.
Source organism: Francisella tularensis subsp. tularensis SCHU S4
Primary publication:
Adherence to Bürgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes.
Light SH, Minasov G, Duban ME, Anderson WF
Acta Crystallogr D Biol Crystallogr 70 544-52 (2014)
PMID: 24531488

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-177676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transaldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 345 amino acids
Theoretical weight: 38.48 KDa
Source organism: Francisella tularensis subsp. tularensis SCHU S4
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5NFX0 (Residues: 1-321; Coverage: 100%)
Gene names: FTT_1093c, talA
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 54.761Å b: 87.019Å c: 140.688Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.151 0.189
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Kinetic Optimization of Lysine-Targeting Covalent Inhibitors of HSP72.
Pettinger et al. (2019)
10 more

1 mention without citation

Adherence to Bürgi-Dunitz stereochemical principles requires significant structural rearrangements in Schiff-base formation: insights from transaldolase complexes.
Light et al. (2014)