› 1k8x

X-ray diffraction
1.9Å resolution

Crystal Structure Of AlphaT183V Mutant Of Tryptophan Synthase From Salmonella Typhimurium

Released:
DOI: 10.2210/pdb1k8x/pdb
PDB entry 1k8x coloured by chain, front view.
PDB entry 1k8x coloured by chain, side view.
PDB entry 1k8x coloured by chain, top view.
Source organisms:
Primary publication:
On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase.
Kulik V, Weyand M, Seidel R, Niks D, Arac D, Dunn MF, Schlichting I
J Mol Biol 324 677-90 (2002)
PMID: 12460570

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: 42.92 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
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 NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: C2
Unit cell:
a: 182.22Å b: 59.99Å c: 67.07Å
α: 90° β: 94.68° γ: 90°
R-values:
R R work R free
0.192 0.192 0.232
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

1 mention without citation

Computational Analysis on the Allostery of Tryptophan Synthase: Relationship between α/β-Ligand Binding and Distal Domain Closure.
Ito et al. (2022)