› 1uin

X-ray diffraction
2.25Å resolution

Crystal Structure of Threonine Synthase from Thermus Thermophilus HB8, Trigonal Crystal Form

Released:
DOI: 10.2210/pdb1uin/pdb
PDB entry 1uin coloured by chain, front view.
PDB entry 1uin coloured by chain, side view.
PDB entry 1uin coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Crystal structures of threonine synthase from Thermus thermophilus HB8: conformational change, substrate recognition, and mechanism.
Omi R, Goto M, Miyahara I, Mizuguchi H, Hayashi H, Kagamiyama H, Hirotsu K
J Biol Chem 278 46035-45 (2003)
PMID: 12952961

Function and Biology Details

Reaction catalysed: 
O-phospho-L-homoserine + H(2)O = L-threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-160757 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 351 amino acids
Theoretical weight: 37.05 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P83823 (Residues: 1-351; Coverage: 100%)
Gene name: TthHB5018_04960
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL40B2
Spacegroup: P3221
Unit cell:
a: 113.207Å b: 113.207Å c: 150.346Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.191 0.219
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The aspartic acid metabolic pathway, an exciting and essential pathway in plants.
Azevedo et al. (2006)
2 more

3 mentions without citation

A Survey of Pyridoxal 5'-Phosphate-Dependent Proteins in the Gram-Positive Model Bacterium Bacillus subtilis.
Richts et al. (2019)
2 more