› 1fxq

X-ray diffraction
1.8Å resolution

AQUIFEX AEOLICUS KDO8P SYNTHASE IN COMPLEX WITH PEP AND A5P

Released:
DOI: 10.2210/pdb1fxq/pdb
PDB entry 1fxq coloured by chain, front view.
PDB entry 1fxq coloured by chain, side view.
PDB entry 1fxq coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Substrate and metal complexes of 3-deoxy-D-manno-octulosonate-8-phosphate synthase from Aquifex aeolicus at 1.9-A resolution. Implications for the condensation mechanism.
Duewel HS, Radaev S, Wang J, Woodard RW, Gatti DL
J Biol Chem 276 8393-402 (2001)
PMID: 11115499

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate + D-arabinose 5-phosphate + H(2)O = 3-deoxy-D-manno-octulosonate 8-phosphate + 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-130317 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-dehydro-3-deoxyphosphooctonate aldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 267 amino acids
Theoretical weight: 29.77 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O66496 (Residues: 1-267; Coverage: 100%)
Gene names: aq_085, kdsA
Sequence domains: DAHP synthetase I family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand PEP 2 x PEP
Ligand A5P 2 x A5P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3121
Unit cell:
a: 84.445Å b: 84.445Å c: 160.057Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.213 0.213 0.233
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Kdo: a critical monosaccharide for bacteria viability.
Cipolla et al. (2010)
1 more

1 mention without citation

Computational Investigation of Bisphosphate Inhibitors of 3-Deoxy-d-manno-octulosonate 8-phosphate Synthase.
Araújo et al. (2019)