› 1c8v

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLTHIO)-BUTYLPHOSPHONIC ACID

Released:
DOI: 10.2210/pdb1c8v/pdb
PDB entry 1c8v coloured by chain, front view.
PDB entry 1c8v coloured by chain, side view.
PDB entry 1c8v coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase.
Sachpatzidis A, Dealwis C, Lubetsky JB, Liang PH, Anderson KS, Lolis E
Biochemistry 38 12665-74 (1999)
PMID: 10504236

Function and Biology Details

Reaction catalysed: 
(1a) 1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133696 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tryptophan synthase alpha chain Chain: A
Molecule details ›
Chain: A
Length: 268 amino acids
Theoretical weight: 28.7 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P00929 (Residues: 1-268; Coverage: 100%)
Gene names: STM1727, trpA
Sequence domains: Tryptophan synthase alpha chain
Structure domains: Aldolase class I
Tryptophan synthase beta chain Chain: B
Molecule details ›
Chain: B
Length: 397 amino acids
Theoretical weight: 42.99 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A2K1 (Residues: 1-397; Coverage: 100%)
Gene names: STM1726, trpB
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
2 bound ligands:
Ligand HE1 1 x HE1
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 183.8Å b: 60.77Å c: 68.15Å
α: 90° β: 94.38° γ: 90°
R-values:
R R work R free
0.212 0.208 0.268
Expression system: Escherichia coli

Quick links

Citations

5 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)
4 more