› 2vlf

X-ray diffraction
1.89Å resolution

Quinonoid intermediate of Citrobacter freundii tyrosine phenol-lyase formed with alanine

Released:
DOI: 10.2210/pdb2vlf/pdb
PDB entry 2vlf coloured by chain, front view.
PDB entry 2vlf coloured by chain, side view.
PDB entry 2vlf coloured by chain, top view.
Source organism: Citrobacter freundii
Primary publication:
Insights into the catalytic mechanism of tyrosine phenol-lyase from X-ray structures of quinonoid intermediates.
Milić D, Demidkina TV, Faleev NG, Matković-Calogović D, Antson AA
J Biol Chem 283 29206-14 (2008)
PMID: 18715865

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151875 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine phenol-lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 456 amino acids
Theoretical weight: 51.57 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli
UniProt:
  • Canonical: P31013 (Residues: 1-456; Coverage: 100%)
Gene name: tpl
Sequence domains: Beta-eliminating lyase
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand PLI 2 x PLI
Ligand PGE 1 x PGE
Ligand K 2 x K
Ligand P33 1 x P33
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P21212
Unit cell:
a: 132.846Å b: 143.687Å c: 59.618Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.157 0.198
Expression system: Escherichia coli

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Citations

2 review citations

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

2 mentions without citation

Insights into the catalytic mechanism of tyrosine phenol-lyase from X-ray structures of quinonoid intermediates.
Milić et al. (2008)
1 more