› 2oqx

X-ray diffraction
1.9Å resolution

Crystal Structure of the apo form of E. coli tryptophanase at 1.9 A resolution

Released:
DOI: 10.2210/pdb2oqx/pdb
PDB entry 2oqx coloured by chain, front view.
PDB entry 2oqx coloured by chain, side view.
PDB entry 2oqx coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation.
Tsesin N, Kogan A, Gdalevsky GY, Himanen JP, Cohen-Luria R, Parola AH, Goldgur Y, Almog O
Acta Crystallogr D Biol Crystallogr 63 969-74 (2007)
PMID: 17704565

Function and Biology Details

Reaction catalysed: 
(1a) L-tryptophan = indole + 2-aminoprop-2-enoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178367 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophanase Chain: A
Molecule details ›
Chain: A
Length: 467 amino acids
Theoretical weight: 52.46 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: Q5UES8 (Residues: 10-476; Coverage: 98%)
Gene name: tnaA
Sequence domains: Beta-eliminating lyase
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: F222
Unit cell:
a: 118.422Å b: 120.116Å c: 171.209Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.203 0.232

Quick links

Citations

2 review citations

The role of substrate strain in the mechanism of the carbon-carbon lyases.
Phillips et al. (2014)
1 more

7 mentions without citation

In vivo protein interaction network identified with a novel real-time cross-linked peptide identification strategy.
Weisbrod et al. (2013)
6 more