› 2cll

X-ray diffraction
1.6Å resolution

Tryptophan Synthase (external aldimine state) in complex with N-(4'- trifluoromethoxybenzenesulfonyl)-2-amino-1-ethylphosphate (F9)

Released:
DOI: 10.2210/pdb2cll/pdb
PDB entry 2cll coloured by chain, front view.
PDB entry 2cll coloured by chain, side view.
PDB entry 2cll coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Allosteric regulation of substrate channeling in tryptophan synthase: modulation of the L-serine reaction in stage I of the beta-reaction by alpha-site ligands.
Ngo H, Kimmich N, Harris R, Niks D, Blumenstein L, Kulik V, Barends TR, Schlichting I, Dunn MF
Biochemistry 46 7740-53 (2007)
PMID: 17559232

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: 396 amino acids
Theoretical weight: 42.79 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A2K1 (Residues: 2-397; Coverage: 100%)
Gene names: STM1726, trpB
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
Ligand F9F 1 x F9F
Ligand PLS 1 x PLS
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2
Unit cell:
a: 182.53Å b: 59.77Å c: 67.34Å
α: 90° β: 94.66° γ: 90°
R-values:
R R work R free
0.217 0.217 0.245
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Tryptophan synthase: the workings of a channeling nanomachine.
Dunn et al. (2008)
4 more

6 mentions without citation

Allosteric regulation of substrate channeling and catalysis in the tryptophan synthase bienzyme complex.
Dunn MF. (2012)
5 more