› 2yct

X-ray diffraction
2.25Å resolution

Tyrosine phenol-lyase from Citrobacter freundii in complex with pyridine N-oxide and the quinonoid intermediate formed with L-alanine

Released:
DOI: 10.2210/pdb2yct/pdb
PDB entry 2yct coloured by chain, front view.
PDB entry 2yct coloured by chain, side view.
PDB entry 2yct coloured by chain, top view.
Source organism: Citrobacter freundii
Primary publication:
Crystallographic snapshots of tyrosine phenol-lyase show that substrate strain plays a role in C-C bond cleavage.
Milić D, Demidkina TV, Faleev NG, Phillips RS, Matković-Čalogović D, Antson AA
OpenAccess logo J Am Chem Soc 133 16468-76 (2011)
PMID: 21899319

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


Cofactor: Ligand PLP 2 x PLP
5 bound ligands:
Ligand PLI 1 x PLI
Ligand K 2 x K
Ligand 9PO 3 x 9PO
Ligand PO4 1 x PO4
Ligand P33 1 x P33
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 133.993Å b: 143.77Å c: 60.081Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.14 0.139 0.181
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Sweet siblings with different faces: the mechanisms of FBP and F6P aldolase, transaldolase, transketolase and phosphoketolase revisited in light of recent structural data.
Tittmann K. (2014)
3 more

1 mention without citation

Crystallographic snapshots of tyrosine phenol-lyase show that substrate strain plays a role in C-C bond cleavage.
Milić et al. (2011)