› 4c1l

X-ray diffraction
1.8Å resolution

Crystal structure of pyrococcus furiosus 3-deoxy-D-arabino- heptulosonate 7-phosphate synthase I181D interface mutant

Released:
DOI: 10.2210/pdb4c1l/pdb
PDB entry 4c1l coloured by chain, front view.
PDB entry 4c1l coloured by chain, side view.
PDB entry 4c1l coloured by chain, top view.
Source organism: Pyrococcus furiosus
Primary publication:
Destabilization of the homotetrameric assembly of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from the hyperthermophile Pyrococcus furiosus enhances enzymatic activity.
Nazmi AR, Schofield LR, Dobson RC, Jameson GB, Parker EJ
J Mol Biol 426 656-73 (2014)
PMID: 24239948

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186379 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DAHP synthetase I/KDSA domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 262 amino acids
Theoretical weight: 29.26 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8U0A9 (Residues: 1-262; Coverage: 100%)
Gene name: PF1690
Sequence domains: DAHP synthetase I family
Structure domains: Aldolase class I

Ligands and Environments

4 bound ligands:
Ligand MN 2 x MN
Ligand CL 4 x CL
Ligand K 2 x K
Ligand 1PE 1 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: I222
Unit cell:
a: 87.942Å b: 110.923Å c: 143.531Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.183
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 citation in other articles

Exploring modular allostery via interchangeable regulatory domains.
Fan et al. (2018)
6 more

1 mention without citation

Domain cross-talk within a bifunctional enzyme provides catalytic and allosteric functionality in the biosynthesis of aromatic amino acids.
Bai et al. (2019)