› 2o78

X-ray diffraction
1.9Å resolution

Tyrosine ammonia-lyase from Rhodobacter sphaeroides (His89Phe variant) complexed with cinnamic acid

Released:
DOI: 10.2210/pdb2o78/pdb
PDB entry 2o78 coloured by chain, front view.
PDB entry 2o78 coloured by chain, side view.
PDB entry 2o78 coloured by chain, top view.
Source organism: Cereibacter sphaeroides
Primary publication:
Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.
Louie GV, Bowman ME, Moffitt MC, Baiga TJ, Moore BS, Noel JP
Chem Biol 13 1327-38 (2006)
PMID: 17185228

Function and Biology Details

Reaction catalysed: 
L-tyrosine = trans-p-hydroxycinnamate + ammonia
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-174582 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine ammonia-lyase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 521 amino acids
Theoretical weight: 54.95 KDa
Source organism: Cereibacter sphaeroides
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q3IWB0 (Residues: 1-523; Coverage: 100%)
Gene names: RSP_3574, hutH
Sequence domains: Aromatic amino acid lyase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand TCA 8 x TCA
1 modified residue:
Ligand MDO 8 x MDO

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21
Unit cell:
a: 87.592Å b: 155.048Å c: 164.044Å
α: 90° β: 94.24° γ: 90°
R-values:
R R work R free
0.172 0.172 0.196
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Phenylpropanoid biosynthesis.
Vogt T. (2010)
12 more

3 mentions without citation

Structural determinants and modulation of substrate specificity in phenylalanine-tyrosine ammonia-lyases.
Louie et al. (2006)
2 more