› 1w3i

X-ray diffraction
1.7Å resolution

Sulfolobus solfataricus 2-keto-3-deoxygluconate (KDG) aldolase complex with pyruvate

Released:
DOI: 10.2210/pdb1w3i/pdb
PDB entry 1w3i coloured by chain, front view.
PDB entry 1w3i coloured by chain, side view.
PDB entry 1w3i coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus.
Theodossis A, Walden H, Westwick EJ, Connaris H, Lamble HJ, Hough DW, Danson MJ, Taylor GL
J Biol Chem 279 43886-92 (2004)
PMID: 15265860

Function and Biology Details

Reaction catalysed: 
2-dehydro-3-deoxy-6-phospho-D-galactonate = pyruvate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129490 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 293 amino acids
Theoretical weight: 33.02 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O54288 (Residues: 2-294; Coverage: 100%)
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand PYR 4 x PYR
Ligand GOL 10 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 83.682Å b: 130.988Å c: 132.293Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.176 0.211
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Enzyme promiscuity: a mechanistic and evolutionary perspective.
Khersonsky et al. (2010)
9 more

3 mentions without citation

Structure and function of aldopentose catabolism enzymes involved in oxidative non-phosphorylative pathways.
Ren et al. (2022)
2 more