› 3czo

X-ray diffraction
2.2Å resolution

Crystal Structure of Double Mutant Phenylalanine Ammonia-Lyase From Anabaena Variabilis

Released:
DOI: 10.2210/pdb3czo/pdb
PDB entry 3czo coloured by chain, front view.
PDB entry 3czo coloured by chain, side view.
PDB entry 3czo coloured by chain, top view.
Source organism: Trichormus variabilis
Primary publication:
Structural and biochemical characterization of the therapeutic Anabaena variabilis phenylalanine ammonia lyase.
Wang L, Gamez A, Archer H, Abola EE, Sarkissian CN, Fitzpatrick P, Wendt D, Zhang Y, Vellard M, Bliesath J, Bell SM, Lemontt JF, Scriver CR, Stevens RC
J Mol Biol 380 623-35 (2008)
PMID: 18556022

Function and Biology Details

Reaction catalysed: 
L-phenylalanine = trans-cinnamate + ammonia
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174748 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phenylalanine ammonia-lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 539 amino acids
Theoretical weight: 59.65 KDa
Source organism: Trichormus variabilis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3M5Z3 (Residues: 25-565; Coverage: 95%)
Gene name: Ava_3988
Sequence domains: Aromatic amino acid lyase
Structure domains:

Ligands and Environments

No bound ligands
2 modified residues:
Ligand MSE 60 x MSE
Ligand MDO 4 x MDO

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2
Unit cell:
a: 195.153Å b: 78.054Å c: 156.758Å
α: 90° β: 120.43° γ: 90°
R-values:
R R work R free
0.214 0.21 0.276
Expression system: Escherichia coli

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Citations

6 review citations

Priming ammonia lyases and aminomutases for industrial and therapeutic applications.
Heberling et al. (2013)
5 more

6 mentions without citation

Structural and biochemical characterization of the therapeutic Anabaena variabilis phenylalanine ammonia lyase.
Wang et al. (2008)
5 more