› 1ngs

X-ray diffraction
2.4Å resolution

COMPLEX OF TRANSKETOLASE WITH THIAMIN DIPHOSPHATE, CA2+ AND ACCEPTOR SUBSTRATE ERYTHROSE-4-PHOSPHATE

Released:
DOI: 10.2210/pdb1ngs/pdb
PDB entry 1ngs coloured by chain, front view.
PDB entry 1ngs coloured by chain, side view.
PDB entry 1ngs coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis.
Nilsson U, Meshalkina L, Lindqvist Y, Schneider G
J Biol Chem 272 1864-9 (1997)
PMID: 8999873

Function and Biology Details

Reaction catalysed: 
Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149906 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transketolase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 680 amino acids
Theoretical weight: 73.89 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P23254 (Residues: 1-680; Coverage: 100%)
Gene names: TKL1, YP9499.29C, YPR074C
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand TPP 2 x TPP
2 bound ligands:
Ligand CA 2 x CA
Ligand E4P 2 x E4P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 76.5Å b: 113.3Å c: 160.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.239
Expression system: Saccharomyces cerevisiae

Quick links

Citations

9 review citations

Properties and functions of the thiamin diphosphate dependent enzyme transketolase.
Schenk et al. (1998)
8 more

3 mentions without citation

Structure and function of the transketolase from Mycobacterium tuberculosis and comparison with the human enzyme.
Fullam et al. (2012)
2 more