› 2v0y

X-ray diffraction
2Å resolution

Crystal structure of apo C298S tryptophanase from E.coli

Released:
DOI: 10.2210/pdb2v0y/pdb
PDB entry 2v0y coloured by chain, front view.
PDB entry 2v0y coloured by chain, side view.
PDB entry 2v0y coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Conformational changes and loose packing promote E. coli Tryptophanase cold lability.
Kogan A, Gdalevsky GY, Cohen-Luria R, Goldgur Y, Phillips RS, Parola AH, Almog O
BMC Struct Biol 9 65 (2009)
PMID: 19814824

Function and Biology Details

Reaction catalysed: 
(1a) L-tryptophan = indole + 2-aminoprop-2-enoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141663 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophanase Chain: A
Molecule details ›
Chain: A
Length: 467 amino acids
Theoretical weight: 52.37 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A853 (Residues: 5-471; Coverage: 99%)
Gene names: JW3686, b3708, ind, tnaA
Sequence domains: Beta-eliminating lyase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CL 1 x CL
Ligand MG 1 x MG
1 modified residue:
Ligand CME 1 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: F222
Unit cell:
a: 120.484Å b: 118.77Å c: 171.534Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.257
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Indole production by the tryptophanase TnaA in Escherichia coli is determined by the amount of exogenous tryptophan.
Li et al. (2013)
4 more

1 mention without citation

Conformational changes and loose packing promote E. coli Tryptophanase cold lability.
Kogan et al. (2009)