› 2yce

X-ray diffraction
1.93Å resolution

Structure of an Archaeal fructose-1,6-bisphosphate aldolase with the catalytic Lys covalently bound to the carbinolamine intermediate of the substrate.

Released:
DOI: 10.2210/pdb2yce/pdb
PDB entry 2yce coloured by chain, front view.
PDB entry 2yce coloured by chain, side view.
PDB entry 2yce coloured by chain, top view.
Source organism: Thermoproteus tenax
Primary publication:
Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates.
Lorentzen E, Siebers B, Hensel R, Pohl E
Biochemistry 44 4222-9 (2005)
PMID: 15766250

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 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 M2P 10 x M2P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 82.9Å b: 159.2Å c: 101.4Å
α: 90° β: 107.8° γ: 90°
R-values:
R R work R free
0.157 0.156 0.198
Expression system: Escherichia coli BL21(DE3)

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Citations

7 review citations

Autotrophic carbon fixation in archaea.
Berg et al. (2010)
6 more