› 3oex

X-ray diffraction
1.9Å resolution

Crystal Structure of Type I 3-Dehydroquinate Dehydratase (aroD) from Salmonella typhimurium with close loop conformation.

Released:
DOI: 10.2210/pdb3oex/pdb
PDB entry 3oex coloured by chain, front view.
PDB entry 3oex coloured by chain, side view.
PDB entry 3oex coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding.
Light SH, Minasov G, Shuvalova L, Peterson SN, Caffrey M, Anderson WF, Lavie A
Biochemistry 50 2357-63 (2011)
PMID: 21291284

Function and Biology Details

Reaction catalysed: 
3-dehydroquinate = 3-dehydroshikimate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157711 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-dehydroquinate dehydratase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 255 amino acids
Theoretical weight: 27.63 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P58687 (Residues: 1-252; Coverage: 100%)
Gene names: STM1358, aroD
Sequence domains: Type I 3-dehydroquinase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand CL 4 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 64.147Å b: 75.757Å c: 94.263Å
α: 90° β: 102.65° γ: 90°
R-values:
R R work R free
0.154 0.152 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 citation in other articles

Crystal structures of type I dehydroquinate dehydratase in complex with quinate and shikimate suggest a novel mechanism of Schiff base formation.
Light et al. (2014)
7 more

1 mention without citation

A conserved surface loop in type I dehydroquinate dehydratases positions an active site arginine and functions in substrate binding.
Light et al. (2011)