› 1ttp

X-ray diffraction
2.3Å resolution

TRYPTOPHAN SYNTHASE (E.C.4.2.1.20) IN THE PRESENCE OF CESIUM, ROOM TEMPERATURE

Released:
DOI: 10.2210/pdb1ttp/pdb
PDB entry 1ttp coloured by chain, front view.
PDB entry 1ttp coloured by chain, side view.
PDB entry 1ttp coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Exchange of K+ or Cs+ for Na+ induces local and long-range changes in the three-dimensional structure of the tryptophan synthase alpha2beta2 complex.
Rhee S, Parris KD, Ahmed SA, Miles EW, Davies DR
Biochemistry 35 4211-21 (1996)
PMID: 8672457

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
1 bound ligand:
Ligand CS 2 x CS
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 185.3Å b: 61.3Å c: 68.1Å
α: 90° β: 94.8° γ: 90°
R-values:
R R work R free
0.217 0.217 0.302
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Structure, evolution and action of vitamin B6-dependent enzymes.
Jansonius JN. (1998)
15 more

1 mention without citation

Tryptophan synthase: structure and function of the monovalent cation site.
Dierkers et al. (2009)