› 2g5c

X-ray diffraction
1.9Å resolution

Crystal Structure of Prephenate Dehydrogenase from Aquifex aeolicus

Released:
DOI: 10.2210/pdb2g5c/pdb
PDB entry 2g5c coloured by chain, front view.
PDB entry 2g5c coloured by chain, side view.
PDB entry 2g5c coloured by chain, top view.
Source organism: Aquifex aeolicus VF5
Primary publication:
Crystal structure of prephenate dehydrogenase from Aquifex aeolicus. Insights into the catalytic mechanism.
Sun W, Singh S, Zhang R, Turnbull JL, Christendat D
J Biol Chem 281 12919-28 (2006)
PMID: 16513644

Function and Biology Details

Reaction catalysed: 
Prephenate + NAD(+) = 4-hydroxyphenylpyruvate + CO(2) + NADH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130524 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prephenate/arogenate dehydrogenase domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 281 amino acids
Theoretical weight: 31.98 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O67636 (Residues: 30-310; Coverage: 90%)
Gene names: aq_1755, tyrA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
No bound ligands
1 modified residue:
Ligand MSE 32 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 42.707Å b: 178.952Å c: 75.195Å
α: 90° β: 99.15° γ: 90°
R-values:
R R work R free
0.22 0.22 0.261
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Cohesion group approach for evolutionary analysis of TyrA, a protein family with wide-ranging substrate specificities.
Bonner et al. (2008)
10 other articles

2 mentions without citation

The crystal structure of Aquifex aeolicus prephenate dehydrogenase reveals the mode of tyrosine inhibition.
Sun et al. (2009)
1 more