› 1xal

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF STAPHLYOCOCCUS AUREUS 3-DEHYDROQUINATE SYNTHASE (DHQS) IN COMPLEX WITH ZN2+, NAD+ AND CARBAPHOSPHONATE (SOAK)

Released:
DOI: 10.2210/pdb1xal/pdb
PDB entry 1xal coloured by chain, front view.
PDB entry 1xal coloured by chain, side view.
PDB entry 1xal coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Comparison of ligand-induced conformational changes and domain closure mechanisms, between prokaryotic and eukaryotic dehydroquinate synthases.
Nichols CE, Ren J, Leslie K, Dhaliwal B, Lockyer M, Charles I, Hawkins AR, Stammers DK
J Mol Biol 343 533-46 (2004)
PMID: 15465043

Function and Biology Details

Reaction catalysed: 
3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179666 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-dehydroquinate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 354 amino acids
Theoretical weight: 40.36 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6GGU4 (Residues: 1-354; Coverage: 100%)
Gene names: SAR1476, aroB
Sequence domains: 3-dehydroquinate synthase
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
2 bound ligands:
Ligand ZN 2 x ZN
Ligand CRB 2 x CRB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P43
Unit cell:
a: 55.1Å b: 55.1Å c: 232.319Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.265
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The shikimate pathway: review of amino acid sequence, function and three-dimensional structures of the enzymes.
Mir et al. (2015)
12 other articles

1 mention without citation

Molecular analysis and essentiality of Aro1 shikimate biosynthesis multi-enzyme in Candida albicans.
Stogios et al. (2022)