› 1ay0

X-ray diffraction
2.6Å resolution

IDENTIFICATION OF CATALYTICALLY IMPORTANT RESIDUES IN YEAST TRANSKETOLASE

Released:
DOI: 10.2210/pdb1ay0/pdb
PDB entry 1ay0 coloured by chain, front view.
PDB entry 1ay0 coloured by chain, side view.
PDB entry 1ay0 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Identification of catalytically important residues in yeast transketolase.
Wikner C, Nilsson U, Meshalkina L, Udekwu C, Lindqvist Y, Schneider G
Biochemistry 36 15643-9 (1997)
PMID: 9398292

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: 73.82 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
1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 76.1Å b: 113.6Å c: 162Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.263
Expression system: Saccharomyces cerevisiae

Quick links

Citations

5 review citations

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

4 mentions without citation

Structural studies of thiamin monophosphate kinase in complex with substrates and products.
McCulloch et al. (2008)
3 more