› 3ggo

X-ray diffraction
2.15Å resolution

Crystal structure of prephenate dehydrogenase from A. aeolicus with HPP and NADH

Released:
DOI: 10.2210/pdb3ggo/pdb
PDB entry 3ggo coloured by chain, front view.
PDB entry 3ggo coloured by chain, side view.
PDB entry 3ggo coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
The crystal structure of Aquifex aeolicus prephenate dehydrogenase reveals the mode of tyrosine inhibition.
Sun W, Shahinas D, Bonvin J, Hou W, Kimber MS, Turnbull J, Christendat D
J Biol Chem 284 13223-32 (2009)
PMID: 19279014

Function and Biology Details

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-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: 314 amino acids
Theoretical weight: 35.26 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O67636 (Residues: 19-311; Coverage: 94%)
Gene names: aq_1755, tyrA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NAI 4 x NAI
Ligand ENO 2 x ENO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 82.496Å b: 92.481Å c: 164.083Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.218 0.262
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Relaxation of tyrosine pathway regulation underlies the evolution of betalain pigmentation in Caryophyllales.
Lopez-Nieves et al. (2018)
7 more

3 mentions without citation

Prediction of homoprotein and heteroprotein complexes by protein docking and template-based modeling: A CASP-CAPRI experiment.
Lensink et al. (2016)
2 more