› 1xag

X-ray diffraction
2.45Å resolution

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

Released:
DOI: 10.2210/pdb1xag/pdb
PDB entry 1xag coloured by chain, front view.
PDB entry 1xag coloured by chain, side view.
PDB entry 1xag 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 Chain: A
Molecule details ›
Chain: A
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 1 x NAD
3 bound ligands:
Ligand ZN 1 x ZN
Ligand CL 5 x CL
Ligand CRB 1 x CRB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P43212
Unit cell:
a: 53.29Å b: 53.29Å c: 240.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.268
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)
11 other articles

3 mentions without citation

Structure and Evolution of the Archaeal Lipid Synthesis Enzyme sn-Glycerol-1-phosphate Dehydrogenase.
Carbone et al. (2015)
2 more