› 4hpx

X-ray diffraction
1.65Å resolution

Crystal structure of Tryptophan Synthase at 1.65 A resolution in complex with alpha aminoacrylate E(A-A) and benzimidazole in the beta site and the F9 inhibitor in the alpha site

Released:
DOI: 10.2210/pdb4hpx/pdb
PDB entry 4hpx coloured by chain, front view.
PDB entry 4hpx coloured by chain, side view.
PDB entry 4hpx coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Allostery and substrate channeling in the tryptophan synthase bienzyme complex: evidence for two subunit conformations and four quaternary states.
Niks D, Hilario E, Dierkers A, Ngo H, Borchardt D, Neubauer TJ, Fan L, Mueller LJ, Dunn MF
Biochemistry 52 6396-411 (2013)
PMID: 23952479

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 analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-133694 (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: 42.92 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

6 bound ligands:
Ligand F9F 1 x F9F
Ligand PEG 5 x PEG
Ligand BZI 3 x BZI
Ligand 0JO 1 x 0JO
Ligand BCN 3 x BCN
Ligand CS 2 x CS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 183.96Å b: 60.96Å c: 67.41Å
α: 90° β: 94.58° γ: 90°
R-values:
R R work R free
0.144 0.142 0.19
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Allosteric crosstalk in modular proteins: Function fine-tuning and drug design.
Abhishek et al. (2023)
23 other articles

10 mentions without citation

Allosteric regulation of substrate channeling: Salmonella typhimurium tryptophan synthase.
Ghosh et al. (2022)
9 more