› 3pg9

X-ray diffraction
2.35Å resolution

Thermotoga maritima DAH7P synthase in complex with inhibitor

Released:
DOI: 10.2210/pdb3pg9/pdb
PDB entry 3pg9 coloured by chain, front view.
PDB entry 3pg9 coloured by chain, side view.
PDB entry 3pg9 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Tyrosine latching of a regulatory gate affords allosteric control of aromatic amino acid biosynthesis.
Cross PJ, Dobson RC, Patchett ML, Parker EJ
J Biol Chem 286 10216-24 (2011)
PMID: 21282100

Function and Biology Details

Reaction catalysed: 
Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194513 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospho-2-dehydro-3-deoxyheptonate aldolase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 338 amino acids
Theoretical weight: 37.43 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYH8 (Residues: 1-338; Coverage: 100%)
Gene names: TM_0343, aroF
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand TYR 8 x TYR
Ligand AZI 2 x AZI
Ligand NO3 4 x NO3
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P21
Unit cell:
a: 81.61Å b: 121.002Å c: 133.379Å
α: 90° β: 92.12° γ: 90°
R-values:
R R work R free
0.172 0.171 0.222
Expression system: Escherichia coli

Quick links

Citations

3 review citations

A Three-Ring Circus: Metabolism of the Three Proteogenic Aromatic Amino Acids and Their Role in the Health of Plants and Animals.
Parthasarathy et al. (2018)
2 more

8 mentions without citation

X-ray Scattering Studies of Protein Structural Dynamics.
Meisburger et al. (2017)
7 more