› 2tpl

X-ray diffraction
2.5Å resolution

TYROSINE PHENOL-LYASE FROM CITROBACTER INTERMEDIUS COMPLEX WITH 3-(4'-HYDROXYPHENYL)PROPIONIC ACID, PYRIDOXAL-5'-PHOSPHATE AND CS+ ION

Released:
DOI: 10.2210/pdb2tpl/pdb
PDB entry 2tpl coloured by chain, front view.
PDB entry 2tpl coloured by chain, side view.
PDB entry 2tpl coloured by chain, top view.
Source organism: Citrobacter freundii
Primary publication:
The crystal structure of Citrobacter freundii tyrosine phenol-lyase complexed with 3-(4'-hydroxyphenyl)propionic acid, together with site-directed mutagenesis and kinetic analysis, demonstrates that arginine 381 is required for substrate specificity.
Sundararaju B, Antson AA, Phillips RS, Demidkina TV, Barbolina MV, Gollnick P, Dodson GG, Wilson KS
Biochemistry 36 6502-10 (1997)
PMID: 9174368

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: 51.74 KDa
Source organism: Citrobacter freundii
UniProt:
  • Canonical: P31013 (Residues: 1-456; Coverage: 100%)
Gene name: tpl
Sequence domains: Beta-eliminating lyase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CS 2 x CS
Ligand HPP 1 x HPP
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P21212
Unit cell:
a: 135.07Å b: 143.91Å c: 59.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.263

Quick links

Citations

6 review citations

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

5 mentions without citation

C-S bond cleavage by a polyketide synthase domain.
Ma et al. (2015)
4 more