› 1tpl

X-ray diffraction
2.3Å resolution

THE THREE-DIMENSIONAL STRUCTURE OF TYROSINE PHENOL-LYASE

Released:
DOI: 10.2210/pdb1tpl/pdb
PDB entry 1tpl coloured by chain, front view.
PDB entry 1tpl coloured by chain, side view.
PDB entry 1tpl coloured by chain, top view.
Source organism: Citrobacter intermedius
Primary publication:
Three-dimensional structure of tyrosine phenol-lyase.
Antson AA, Demidkina TV, Gollnick P, Dauter Z, von Tersch RL, Long J, Berezhnoy SN, Phillips RS, Harutyunyan EH, Wilson KS
Biochemistry 32 4195-206 (1993)
PMID: 7916622

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 domain:

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: 51.51 KDa
Source organism: Citrobacter intermedius
Expression system: Not provided
UniProt:
  • Canonical: P31013 (Residues: 1-456; Coverage: 100%)
Gene name: tpl
Sequence domains: Beta-eliminating lyase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 76.02Å b: 138.27Å c: 93.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 not available not available
Expression system: Not provided

Quick links

Citations

9 review citations

Structure, evolution and action of vitamin B6-dependent enzymes.
Jansonius JN. (1998)
8 more

2 mentions without citation

Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions.
Milić et al. (2006)
1 more