› 3s1w

X-ray diffraction
1.8Å resolution

Transaldolase variant Lys86Ala from Thermoplasma acidophilum in complex with glycerol and citrate

Released:
DOI: 10.2210/pdb3s1w/pdb
PDB entry 3s1w coloured by chain, front view.
PDB entry 3s1w coloured by chain, side view.
PDB entry 3s1w coloured by chain, top view.
Source organism: Thermoplasma acidophilum DSM 1728
Primary publication:
Twisted Schiff base intermediates and substrate locale revise transaldolase mechanism.
Lehwess-Litzmann A, Neumann P, Parthier C, Lüdtke S, Golbik R, Ficner R, Tittmann K
Nat Chem Biol 7 678-84 (2011)
PMID: 21857661

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 decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190875 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable transaldolase Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 223 amino acids
Theoretical weight: 24.44 KDa
Source organism: Thermoplasma acidophilum DSM 1728
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HKI3 (Residues: 1-223; Coverage: 100%)
Gene names: Ta0616, tal
Sequence domains: Transaldolase/Fructose-6-phosphate aldolase
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand GOL 5 x GOL
Ligand FLC 5 x FLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: C2221
Unit cell:
a: 145.08Å b: 168.67Å c: 97.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.208
Expression system: Escherichia coli

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Citations

5 review citations

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
4 more