› 3s0c

X-ray diffraction
1.78Å resolution

Transaldolase wt of Thermoplasma acidophilum

Released:
DOI: 10.2210/pdb3s0c/pdb
PDB entry 3s0c coloured by chain, front view.
PDB entry 3s0c coloured by chain, side view.
PDB entry 3s0c 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: 24.49 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

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: C2221
Unit cell:
a: 149.044Å b: 172.024Å c: 100.271Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.229
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