› 1ok6

X-ray diffraction
2.4Å resolution

Orthorhombic crystal form of an Archaeal fructose 1,6-bisphosphate aldolase

Released:
DOI: 10.2210/pdb1ok6/pdb
PDB entry 1ok6 coloured by chain, front view.
PDB entry 1ok6 coloured by chain, side view.
PDB entry 1ok6 coloured by chain, top view.
Source organism: Thermoproteus tenax
Primary publication:
Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins.
Lorentzen E, Pohl E, Zwart P, Stark A, Russell RB, Knura T, Hensel R, Siebers B
J Biol Chem 278 47253-60 (2003)
PMID: 12941964

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157670 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase class 1 Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 263 amino acids
Theoretical weight: 28.74 KDa
Source organism: Thermoproteus tenax
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P58315 (Residues: 1-263; Coverage: 100%)
Gene names: TTX_1278, fba
Sequence domains: DeoC/LacD family 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: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 89.9Å b: 176.5Å c: 185.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.232 0.263
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

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

2 mentions without citation

Cell-cycle-regulated activation of Akt kinase by phosphorylation at its carboxyl terminus.
Liu et al. (2014)
1 more